carboxypeptidase-b and Acute-Disease

Serum levels of amylase and lipase can be elevated in nonpancreatic conditions that may or may not be associated with abdominal pain. This leads to a large proportion of patients being falsely labeled as having acute pancreatitis. In this review, we aim to summarize the existing evidence on pancreatic enzyme elevation in various pancreatic and nonpancreatic conditions and its practical implications in clinical practice and healthcare.. Serum amylase and lipase levels are not specific for pancreatitis. Attempts have been made to validate newer biomarkers including pancreatic elastase, serum trypsin, urinary trypsinogen-activated peptide, phospholipase A2, carboxypeptidase B, activated peptide of carboxypeptidase B, the trypsin 2 alpha 1 activation complex, and circulating cell-free DNA for the diagnosis of acute pancreatitis.. Serum lipase levels can be elevated in many intra-abdominal inflammatory conditions. Although more sensitive and specific than amylase, serum lipase levels are not sufficient to diagnose acute pancreatitis in patients with abdominal pain. There is a need to increase stress on radiological evidence as well increase cut-off levels of enzyme elevation for a more accurate diagnosis of acute pancreatitis.

Topics: Abdominal Pain; Acute Disease; Amylases; Carboxypeptidase B; Humans; Lipase; Pancreatitis; Peptides; Trypsin

A large array of parameters has been proposed for the biochemical stratification of severity and prediction of complications in acute pancreatitis. However, the number of accurate and readily available variables for routine application is still limited.. The literature was reviewed for laboratory markers of acute pancreatitis with special regard to their clinical usefulness and test performance for stratifying severity and monitoring disease progression.. Several parameters, such as trypsinogen and procarboxypeptidase B activation peptide, PMN-elastase, interleukin-6 (IL-6) and 8 (IL-8), serum amyloid A (SAA), and procalcitonin (PCT), can differentiate between mild and severe acute pancreatitis within 48 h of disease onset with favorable diagnostic accuracy. Because fully automated assays have become available, IL-6, IL-8, PCT, and SAA are the most interesting parameters in this respect. For monitoring disease progression beyond 48 h, acute-phase proteins, IL-6, IL-8, and PCT are valuable markers. PCT is the first biochemical variable for predicting severe pancreatic infections and overall prognosis throughout the course of acute pancreatitis with high sensitivity and specificity.. Among all the biochemical variables available, C-reactive protein is still the standard for a fast, reliable, and cost-effective assessment of severity in acute pancreatitis. PCT substantially contributes to an improved stratification of patients at risk to develop major complications and deserves routine application.

Topics: Acute Disease; Biomarkers; Calcitonin; Calcitonin Gene-Related Peptide; Carboxypeptidase B; Disease Progression; Humans; Interleukins; Oligopeptides; Pancreatic Juice; Pancreatitis; Protein Precursors; Serum Amyloid A Protein; Severity of Illness Index

Acute pancreatitis (AP) is a common disease associated with an improper activation of pancreatic zymogens leading to autodigestion of the gland and if excessive--to multiple organ dysfunction. Acute necrotizing pancreatitis manifested by 20% of patients with acute pancreatitis is a life threatening disorder requiring subsequent management in intensive care unit. Unfortunately, none of biochemical tests presently used for laboratory assessment of acute pancreatitis at the early stage of the disease is able to estimate accurately: diagnosis, etiology and severity. At present, diagnosis of acute pancreatitis is based on evaluation of serum amylase and lipase activity due to easy availability and simplicity of these enzymatic tests. Low specificity of the mentioned enzymes resulted in studies concerning pancreatic isoamylase, elastase-1, chymotrypsine, procarboxy-peptidase B, trypsinogen-2 and immunoreactive trypsinogen usefulness in the laboratory diagnosis of AP. The prediction of severity in acute pancreatitis using multifactorial scoring systems is cumbersome especially due to their complexity. On the other hand the biochemical method of choice, estimation of serum C reactive protein, is useless in the early phase of disease. Unfortunately, the computed tomography--the most accurate method in severity assessing--is not always available. Recent studies have brought some progress in severity predicting, such as phospholipase A2, cellular immunity markers, cytokines, activation peptides of trypsinogen and carboxypeptidase B, procalcitonine, pancreatitis associated protein and serum amyloid A. All these newly introduced biochemical methods allow to look optimistically into the future of laboratory diagnostics of the acute pancreatitis believing that the problem of diagnosing and predicting the AP severity will be solved.

Topics: Acute Disease; Biomarkers; Calcitonin; Carboxypeptidase B; Cytokines; Diagnosis, Differential; Humans; Pancreatitis; Pancreatitis-Associated Proteins; Phospholipases A; Phospholipases A2; Protein Precursors; Treatment Outcome

Topics: Acute Disease; Carboxypeptidase B; Carboxypeptidases; Enzyme Activation; Enzyme Precursors; Humans; Oligopeptides; Pancreas; Pancreatitis; Prognosis; Proteins

CAPAP, the activation peptide of procarboxypeptidase B, is a predictor of severe acute pancreatitis (AP). Active carboxypeptidase (aCAP) may be a better predictor, as its turnover is slower. Monocyte chemotactic protein-1 (MCP-1) is an early inflammatory marker and increases before complications in severe AP. We conducted a cohort study to evaluate these markers as predictors for severe AP.. 140 patients with AP were included, retrospectively grouped as severe or mild by the Atlanta classification. CAPAP, MCP-1 and aCAP were analyzed in admission samples. Receiver operating characteristic curves determined high vs. low levels.. The levels of all markers were significantly higher in patients with severe disease. High levels of serum MCP-1 was associated with a high risk of developing severe AP (OR 40.8; 95% CI 8.5-195). High ORs were also seen for urine MCP-1 (OR 7.3; 95% CI 2.2-24.3), serum CAPAP (OR 5.4; 95% CI 1.6-17.7), urine CAPAP (OR 4.8; 95% CI 1.6-14.2), and serum aCAP (OR 3.7; 95% CI 1.2-11.3).. Serum MCP-1 at admission was strongly associated with development of severe AP. MCP-1 in urine, CAPAP in serum and urine and aCAP may also be useful for predicting severe AP. and IAP.

Topics: Acute Disease; Adult; Aged; Aged, 80 and over; Biomarkers; Carboxypeptidase B; Chemokine CCL2; Cohort Studies; Female; Humans; Male; Middle Aged; Pancreatitis; Peptides; Predictive Value of Tests; ROC Curve; Sensitivity and Specificity; Severity of Illness Index

Active carboxypeptidase B (aCAP) is the main product of activation of procarboxypeptidase. The other product derived from procarboxypeptidase B (proCAP), the activation peptide carboxypeptidase B (CAPAP), has been shown to be a marker for severity in acute pancreatitis. There have been relatively few studies dealing with the role of this enzyme in acute pancreatitis.. A double-antibody ELISA for immunoreactive aCAP (ir-aCAP) was developed, and ir-aCAP was determined in the serum of patients with acute pancreatitis and characterized using gel filtration.. Serum from healthy individuals contained minimal levels of ir-aCAP, while serum from 25 patients with acute pancreatitis contained between 0.6 and 158 nmol/l. Gel filtration of serum samples from patients with acute pancreatitis showed the presence of two peaks of ir-aCAP, one corresponding to the molecular size of the free active enzyme and one corresponding to cross-reactive proCAP. When pure aCAP was mixed with serum in vitro, all ir-aCAP was recovered as one peak of free enzyme. No immunoreactivity disappeared or changed in molecular size, as might be expected if the active enzyme was bound to an inhibitor.. aCAP is present in free form in the circulation of patients with acute pancreatitis.

Topics: Acute Disease; C-Reactive Protein; Carboxypeptidase B; Chromatography, Gel; Cross Reactions; Enzyme Activation; Enzyme-Linked Immunosorbent Assay; Pancreatitis; Peptides

Serum and urine concentrations of the activation peptide of carboxypeptidase B (CAPAP) and urinary trypsinogen activation peptide (TAP) as prognostic markers in acute pancreatitis were compared.. Fifty-two patients with acute pancreatitis hospitalized within 24 hours after symptom onset were prospectively studied. Blood and urine samples were obtained during the first 3 days of the hospital stay.. Pancreatitis was severe in 17 patients and mild in 35 (Atlanta criteria). Median serum CAPAP levels on days 1 and 2 and of urine CAPAP and TAP on days 1, 2, and 3 were significantly higher in severe pancreatitis than in mild disease. On the first day of admission, TAP was the most accurate predictor of severity (sensitivity, 92.3%; specificity, 80%; positive and negative predictive values, 63.2% and 96.6%, respectively), with a 4.61 positive likelihood ratio for a cutoff value of 18.10 nmol/L, whereas within 24 hours after symptom onset, urinary CAPAP was superior (sensitivity, 88.9%; specificity, 81.3%; positive and negative predictive values 72.7% and 92.9%, respectively), with a 4.72 positive likelihood ratio for a cutoff value of 15.45 nmol/L.. Serum and urine CAPAP levels and urinary TAP are accurate in the early assessment of severity in acute pancreatitis. Urine CAPAP levels was the most accurate marker 24 hours after onset of symptoms.

Topics: Abdominal Pain; Acute Disease; Adult; Aged; Biomarkers; Carboxypeptidase B; Enzyme Activation; Female; Humans; Male; Middle Aged; Oligopeptides; Pancreatitis; Peptides; Predictive Value of Tests; Prognosis; Prospective Studies; ROC Curve; Severity of Illness Index; Trypsinogen

Carboxypeptidase B from the pancreatic gland may exist in three different molecular and immunoreactive forms: the proenzyme, the active enzyme, and the activation peptide.. To investigate levels of procarboxypeptidase B (proCAPB) and its activation peptide in serum in acute pancreatitis to test the accuracy of these two variables as markers for the diagnosis of acute pancreatitis and for prediction of pancreatic necrosis. To elucidate whether leakage of proenzymes and activation of proenzymes reflect two different pathophysiological events in acute pancreatitis.. Sera from patients with acute pancreatitis (n=85) and acute abdominal pain of non-pancreatic origin (n=53) were analysed for proCAPB and its activation peptide. Patients with pancreatitis were divided into necrotising (n=33) and oedematous attacks (n=52) using contrast enhanced computed tomography. Accuracy was determined using receiver operating characteristic curve analysis.. Immunoreactive carboxypeptidase B activation peptide (ir-CAPAP) concentration in serum on admission was 0.7 nmol/l (0-18.1) in patients with oedematous pancreatitis compared with 5.8 nmol/l (1.9-34) in patients with later development of pancreatic necrosis. Elevated levels of the activation peptide on admission correlated with an accuracy of 92% to later development of pancreatic necrosis. Ir-proCAPB concentration in serum on admission was 16.0 nmol/l (1.4-50.5) in all patients with acute pancreatitis versus 0.3 nmol/l (0-3.6) in patients with non-pancreatic acute abdominal disorders. Cases with oedematous pancreatitis had ir-proCAPB levels of 15.4 nmol/l (1.4-50.5) versus 19.1 nmol/l (2.7-36.1) in cases with later development of pancreatic necrosis. Measurement of the proenzyme can thus be useful for the diagnosis of acute pancreatitis (accuracy 99%) but levels did not correlate with later development of pancreatic necrosis (accuracy 56%).. Leakage of proenzymes occurs in acute pancreatitis, irrespective of severity, while development of pancreatic necrosis occurs only when there is activation of the proenzymes.

Topics: Abdominal Pain; Acute Disease; Adult; Aged; Aged, 80 and over; Biomarkers; Carboxypeptidase B; Carboxypeptidases; Enzyme Activation; Enzyme Precursors; Female; Humans; Male; Middle Aged; Necrosis; Pancreas; Pancreatic Diseases; Pancreatitis; ROC Curve; Statistics, Nonparametric; Tomography, X-Ray Computed

Topics: Acute Disease; Biomarkers; C-Reactive Protein; Carboxypeptidase B; Carboxypeptidases; Clinical Enzyme Tests; Enzyme Activation; Humans; Oligopeptides; Pancreatitis; Peptides; Sensitivity and Specificity; Trypsin; Trypsinogen

A reliable, noninvasive indicator of pancreatic allograft rejection is urgently needed. In this study, serum (S), plasma (P), and urine (U) levels of pancreas-specific protein (P-PASP, U-PASP), neopterin (S-NEOP, U-NEOP), amylase (U-AMYL), and amyloid A (SAA) were measured daily in ten type I diabetic patients following simultaneous pancreas and kidney transplantation (SPK). Rejection episodes occurred in three isolated pancreas, nine isolated kidney, and five simultaneous pancreas and kidney transplants. In the case of the eight pancreas rejections, SAA was the rejection marker with the highest diagnostic accuracy (94%). Using P-PASP and U-PASP, an accuracy of 81% and 79%, respectively, was achieved. During viral infections, U-NEOP levels increased to a maximum level of 1904 mumol/mol creatinine, whereas during bacterial infections, SAA levels increased to a maximum value of 43 mg/dl. SAA, measured for the first time in SPK, appears to be a valuable rejection parameter. In combination with U-NEOP and U-AMYL, a differential diagnosis between rejection, bacterial infection, and viral infection was possible. Neither U-PASP nor P-PASP monitoring led to a significant improvement in the results.

Topics: Acute Disease; Adult; Apolipoproteins; Bacterial Infections; Biopterins; Carboxypeptidase B; Carboxypeptidases; Diabetes Mellitus, Type 1; Female; Graft Rejection; Humans; Kidney Transplantation; Male; Neopterin; Pancreas Transplantation; Pilot Projects; Proteins; Serum Amyloid A Protein; Virus Diseases

Human pancreas-specific protein (PASP) has been characterized previously as a serum marker for pancreatitis. It was then identified as pancreatic procarboxypeptidase B (PCB). The aim of the present study was to verify the usefulness of PASP (PCB) as a serum marker in patients with acute (n = 20) and chronic (n = 12) pancreatitis and in those following endoscopic retrograde cholangiopancreaticography (ERCP) (n = 44). Serum PASP values were analyzed by radioimmunoassay, with a range of normal values between 15 and 111 ng/ml. Between April 1992 and September 1992, 20 subjects (19-86 years of age) with acute pancreatitis (alcoholic, 8; biliary, 8; other, 4) were studied. We found edematous pancreatitis in 17 cases and severe hemorrhagic pancreatitis in three cases. At admission, peak levels of PASP (average value, 1,976 +/- 329 ng/ml), pancreatic isoamylase (942 +/- 151 U/L) and lipase (2,946 +/- 534 U/L) were detected in 15 of 20, 16 of 20, and 12 of 20 cases, respectively. The etiology of the pancreatitis had no influence on the PASP values. Furthermore, 10 patients with alcoholic and two patients with nonalcoholic chronic pancreatitis (29-67 years of age) were studied. The average peak level of PASP was 1,229 +/- 434 ng/ml. In this group, PASP paralleled the time course of amylase and lipase. Maximal PASP, amylase, and lipase levels were found in 11 of 12, nine of 12, and five of 12 patients, respectively, on the day of admission. ERCP was performed in 44 patients (36-87 years of age), demonstrating common bile duct stones in 16 and bile or pancreatic ductal tumors in 15 cases.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Acute Disease; Adult; Aged; Aged, 80 and over; Biomarkers; Carboxypeptidase B; Carboxypeptidases; Cholangiopancreatography, Endoscopic Retrograde; Chronic Disease; Enzyme Precursors; Female; Humans; Isoamylase; Lipase; Male; Middle Aged; Pancreas; Pancreatitis; Proteins

To compare the clinical utility of serum pancreas-specific protein and serum amylase in the diagnosis of acute pancreatitis, the study was conducted in 134 normal subjects and 70 patients (36 with acute pancreatitis and 34 with other acute abdominal diseases as control group). The serum level of pancreas-specific protein in 134 healthy adults was 29.6 +/- 1.6 micrograms/l, with 95% within 7.3-67.2 micrograms/l. The upper reference limit was set at 70 micrograms/l. Serum levels of pancreas-specific protein and amylase within 12 h of arrival were significantly higher in patients with acute pancreatitis than in the control group (647.3 +/- 79.3 versus 33.8 +/- 4.8 micrograms/l (p < 0.0001) and 2536 +/- 344 versus 175 +/- 35 IU/l (p < 0.0001)). No significant difference in the levels of pancreas-specific protein was noted between biliary and alcoholic pancreatitis or between severe and mild attacks. The sensitivity, specificity, and accuracy of diagnosing acute pancreatitis were 100%, 94.1%, and 97.1% with serum pancreas-specific protein > 70 micrograms/l and 97.2%, 91.2%, and 94.3% with serum amylase > 360 IU/l. The result demonstrated that pancreas-specific protein may be a good serum marker in the diagnosis of acute pancreatitis.

Topics: Acute Disease; Adult; Aged; Aged, 80 and over; Amylases; Biomarkers; Carboxypeptidase B; Carboxypeptidases; Female; Humans; Male; Middle Aged; Pancreatitis; Proteins; Sensitivity and Specificity

The aim of this study was to evaluate the serum behavior of human pancreas-specific protein/procarboxypeptidase B (hPASP/PCPB) in the early phases of acute pancreatitis, and to calculate its sensitivity and specificity in comparison with those of serum amylase and lipase in the diagnosis of this illness. Twenty-six acute pancreatitis patients were studied; the pancreatitis was of biliary origin in 11, due to alcohol abuse in 8, and due to other causes in 7. Sixteen patients had mild pancreatitis and 10 the severe form of the disease. Thirty-one patients with nonpancreatic acute digestive diseases were also studied. Serum concentrations of hPASP/PCPB, amylase and lipase were determined in all subjects on admission to the study as well as daily for the following 5 days in acute pancreatitis patients. All patients with acute pancreatitis had abnormally high serum hPASP/PCPB, amylase and lipase concentrations on the first day of admission. On the sixth day of the disease, 76% of acute pancreatitis patients had abnormally high serum concentrations of hPASP/PCPB, whereas only 48% (p < 0.05) had elevated serum amylase and lipase. No differences in serum levels of hPASP/PCPB, amylase or lipase were found between patients with alcoholic pancreatitis and those with other etiological forms of the disease, or between those with mild and severe forms of pancreatitis. The specificity of the three serum pancreatic protein assays, calculated on the 31 patients with nonpancreatic acute digestive diseases, was 90% for both hPASP/PCPB and lipase, 75% for amylase.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Acute Disease; Adolescent; Adult; Aged; Aged, 80 and over; Amylases; Biomarkers; Carboxypeptidase B; Carboxypeptidases; Enzyme Precursors; Female; Humans; Lipase; Male; Middle Aged; Pancreatitis; Proteins; Sensitivity and Specificity

Human Pancreas-Specific Protein (PASP) has been described as a useful serum marker for pancreatic graft rejection and acute pancreatitis. By molecular cloning PASP has recently been identified as procarboxypeptidase B (PCPB). By use of SDS-gel electrophoresis and Western blots, PASP isoforms (proteins interacting with PASP-antiserum) have now been explored in serum and pancreatic tissue and juice. In serum from healthy volunteers, six different isoforms could be visualised. Their MW varied as follows: > 100 K, about 100 K, 45 K, 35-40 K (two bands) about 30 K and 16 K. The 45 K band, corresponding to PASP purified from pancreatic tissue, was always the major band. In pancreatic cytosol and pancreatic juice, the major band corresponded to PASP (45 K) but weak bands were also seen at MW of 40, 30 and 16 K. In serum from 15 patients with acute pancreatitis, PASP was highly increased. Bands corresponding to PASP/PCPB as well as carboxypeptidase B (CPB) were seen simultaneously. During recovery PASP in serum was normalised and the CPB band disappeared. During 12 episodes of pancreatic graft rejection, PASP in serum was also increased but no changes of isoforms in serum were detected. However during these episodes isoforms in pancreatic juice changed dramatically. The band corresponding to PASP disappeared or became much weaker and only bands with lower MW were seen. We have thus observed changes in PASP/PCB serum isoforms during episodes of acute pancreatitis but not at graft rejection episodes although the total increase of PASP in serum was of the same magnitude.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Acute Disease; Carboxypeptidase B; Carboxypeptidases; Cytosol; Enzyme Precursors; Exercise; Graft Rejection; Humans; Isoenzymes; Pancreas; Pancreas Transplantation; Pancreatic Juice; Pancreatitis

A human pancreas-specific protein (PASP), previously characterized as a serum marker for acute pancreatitis and pancreatic graft rejection, has been identified as pancreatic procarboxypeptidase B (PCPB). cDNAs encoding PASP/PCPB were isolated from a human pancreas cDNA library using a combination of nucleic acid hybridization screening and immunoscreening with antisera raised against native PASP. The deduced amino acid sequence of PASP/PCPB cDNA predicts the translation of a 416-amino acid preproenzyme with a 15-amino acid signal/leader peptide and a 95-amino acid activation peptide. The proenzyme portion of this protein has 76% identity with rat PCPB and 84% identity with bovine carboxypeptidase B. DNA and RNA blot analyses indicate that human PCPB mRNA (1,400 nucleotides) is transcribed from a single locus in the human genome in a tissue-specific fashion. N-terminal sequencing of native PASP and the specific immunoreactivity of bacterially expressed PASP/PCPB with native PASP antibodies confirm the identification of PASP as human pancreatic PCPB.

Topics: Acute Disease; Amino Acid Sequence; Base Sequence; Biomarkers; Blotting, Northern; Blotting, Southern; Blotting, Western; Carboxypeptidase B; Carboxypeptidases; DNA; Enzyme Precursors; Humans; Molecular Sequence Data; Nucleic Acid Hybridization; Pancreatitis; Polymerase Chain Reaction; Proteins; RNA; Sequence Alignment; Sequence Homology, Nucleic Acid

Pancreas-specific protein (PASP) was compared with serum amylase in 95 episodes of acute pancreatitis with the diagnoses supported by elevated amylase levels. The etiology was typical for Scandinavian countries, with alcohol as the predominant factor, followed by cholelithiasis. PASP values were clearly raised in all patients, except in three cases found to have high salivary-type amylase levels, and one patient with recurrent alcohol pancreatitis. The rise of PASP levels were in general more pronounced than the corresponding amylase elevations, especially in severe pancreatitis. The elevations were generally parallel for the two analytes, but in 41% of the cases PASP levels remained elevated 2-11 days longer than the corresponding amylase levels. PASP was, however, eliminated from the circulation at a rate comparable to that of amylase. The serum range of PASP for 259 healthy subjects was 15-111 micrograms/L with 95% of the values within 16-98 micrograms/L. The upper reference level was set at 100 micrograms/L. PASP levels were also determined for 291 patients with disorders other than acute pancreatitis. Serum levels in patients with renal insufficiency (n = 12), primary biliary cirrhosis (n = 9), and diabetes mellitus (n = 17) were equal to those in healthy subjects. Eight patients of 173 with acute abdominal disorders and no evidence of pancreatitis had elevated PASP levels as well as 4 patients with prostatic carcinoma (n = 28) and 2 patients with benign prostatic hyperplasia (n = 16). PASP values were low in chronic painful pancreatitis (n = 15) and pancreatic cancer (n = 11).

Topics: Acute Disease; Adult; Age Factors; Aged; Amylases; Biomarkers; Carboxypeptidase B; Carboxypeptidases; Chronic Disease; Diabetes Mellitus; Humans; Male; Middle Aged; Pancreatic Neoplasms; Pancreatitis; Prostatic Hyperplasia; Prostatic Neoplasms; Proteins

Previous studies have suggested that measurement of active enzymes in relation to proenzymes in serum of patients with pancreatitis may reflect the degree of zymogen activation in the gland. Here we describe the first single-tube assay for an active form of a pancreatic enzyme that is ordinarily synthesized as a proenzyme. Human procarboxypeptidase B, which we purified to near homogeneity, is approximately 13 000 Da larger than the active enzyme (EC 3.4.17.2). Antibodies specific for active carboxypeptidase B were obtained by affinity chromatography of anti-carboxypeptidase B antisera on a gel containing procarboxypeptidase B, then used to develop a single-tube radioimmunoassay for measuring active carboxypeptidase B in serum. Using this assay, we were able to detect, for the first time, active carboxypeptidase B in sera from patients with acute pancreatitis. Preliminary data show a correlation between the serum concentrations of active carboxypeptidase B and those of active trypsin complexed with serum inhibitors, but no correlation with serum amylase values.

Topics: Acute Disease; Carboxypeptidase B; Carboxypeptidases; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Enzyme Precursors; Humans; Molecular Weight; Pancreatitis; Radioimmunoassay; Trypsin

Serum carboxypeptidase B (SCPB) levels were measured in splenectomised calves and in non-splenectomised cattle infected with three virulent and one avirulent strains of Babesia bovis, and in splenectomised calves infected with virulent Babesia bigemina parasites. SCPB levels commenced falling three days post-infection in animals infected with virulent B. bovis strains and fell significanttly terminally. In animals infected with the avirulent B. bovis strain, the SCPB levels were not significantly altered. Animals infected with B. bigemina had no significant changes in their SCPB levels. Fatal infections were uniformly observed in animals with virulent B. bovis, but only two of six animals infected with B. bigemina and none infected with avirulent B. bovis, died.

Topics: Acute Disease; Animals; Babesia; Babesiosis; Carboxypeptidase B; Carboxypeptidases; Cattle; Cattle Diseases; Female; Male; Species Specificity; Splenectomy; Virulence