alpha-chymotrypsin and Syndrome

The effect of supplementing a cornsoybean diet (C) with glucose (G) or maltose (M) on young broilers (from hatch to 3 wk of age) affected by stunting syndrome (SS) was studied. Stunting syndrome was induced by orally administering an inoculum prepared from the intestines of SS broiler chicks. Relative to the M diet, the G diet improved growth and feed utilization and increased feed intake in naive (NA) control chickens. The C diet was intermediate in this respect. In contrast to the NA chickens, diet did not affect growth or feed utilization in SS chicks. Changes in the relative weights of the gastrointestinal tract segments were evident by 1 wk of age and hypertrophy of these segments persevered to 3 wk of age. Stunting syndrome infection was accompanied by a significant increase in pancreatic trypsin-specific activity during Weeks 1 and 2, and in chymotrypsin activity at 1 wk. During this time, amylase-specific activity was not affected. At 3 wk of age, the specific activities of amylase, trypsin, and chymotrypsin in the pancreas were lower in the inoculated vs control birds. Whereas no significant effect of SS was observed with activities of amylase in the intestinal contents, trypsin activity was higher in SS chicks at 1 wk, and that of chymotrypsin lower during Weeks 2 and 3. Relative to NA chicks, the maltase and saccharase activities of SS chicks were much lower during Week 1, but increased later on and were similar to NA chick values at 2 and 3 wk. Whereas the level of blood plasma proteins did not vary from 1 to 3 wk in the NA chicks, it increased gradually in SS chicks to a level that significantly exceeded that in their NA counterparts. Blood plasma glucose and triglyceride levels were slightly lower in the SS chicks (NS), and the blood plasma cholesterol level was significantly reduced during Week 2. Relative to NA chicks, SS infection caused a significant increase in plasma calcium during Weeks 2 and 3, accompanied by a significant reduction in blood plasma phosphorus at 2 wk only. No difference was observed in the blood plasma level of uric acid, which peaked in both treatments during Week 2, or in D-beta-hydroxybutyric acid level, which was quite stable during the experimental period. Stunting syndrome infection was accompanied by a dramatic increase in amylase and alkaline phosphatase activities in the blood plasma, and by a slight but significant decrease in activity of lactic dehydrogenase. Stunting syndrome was concluded to be an afflic

Topics: Aging; alpha-Glucosidases; Amylases; Animal Feed; Animals; Blood Proteins; Body Weight; Calcium; Chickens; Chymotrypsin; Digestive System; Eating; Food, Fortified; Glucose; Growth Disorders; Intestinal Mucosa; Intestines; Lipids; Male; Maltose; Organ Size; Phosphorus; Poultry Diseases; Sucrase; Syndrome; Tissue Extracts; Trypsin

Six polypeptides resolved by two-dimensional electrophoresis of homogenates from human skeletal muscle have been identified as tropomyosin by electrophoretic and immunochemical methods. The 6 proteins are consistently present in approximately the same abundance in normal biceps, deltoid, gastrocnemius, and quadriceps muscle. Analysis of samples from individuals with Becker's dystrophy, Duchenne dystrophy, limb girdle dystrophy, polymyositis, myopathy related to vitamin E deficiency, type II fiber deficiency, and from an infant with indistinct fiber type differentiation, however, showed quantitative variations in the tropomyosin pattern. Muscle with histochemically demonstrated type II fiber deficiency lacked two of the normal tropomyosin proteins and the type II myosin light chains. Muscles lacking type I myosin light chains were deficient in a different pair of tropomyosin proteins. The results suggest that normal human skeletal muscle contains one major type of tropomyosin protein (beta-tropomyosin) common to both fast and slow fibers, together with two other major proteins (alpha-tropomyosin and alpha'-tropomyosin), one of which is specific to fast fibers and the other to slow fibers. Preliminary data from the reaction of muscle homogenates with alkaline phosphatase indicate that 3 of the 6 tropomyosin polypeptides resolved by two-dimensional electrophoresis are phosphorylated forms of the alpha-, alpha'-, and beta-tropomyosins.

Topics: Adolescent; Adult; Catalysis; Chemical Phenomena; Chemistry; Child; Chymotrypsin; Electrophoresis; Female; Humans; Male; Middle Aged; Muscles; Muscular Diseases; Muscular Dystrophies; Myofibrils; Peptide Hydrolases; Syndrome; Tropomyosin

Platelet glycoprotein I (GPI) is known to be required for the interaction of platelets with ristocetin and factor VIII:von Willebrand factor (VIII:vWf). However, its role as Fc receptor is not clear. Some studies have shown that enzymatic removal of GPI destroys the ability of platelets to react with VIII:vWf but not their ability to bind Ig G (IgG). Others have shown that IgG immune complexes which block the Fc receptor also inhibit VIII:vWf interaction with platelets. This subject has been re-examined by testing the ability of platelets with reduced amounts of GPI to aggregate and undergo the release reaction in response to stimuli which act at the platelet Fc receptor. Platelets from two patients with Bernard-Soulier syndrome, congenitally deficient in GPI, both aggregated and released 14C-serotonin normally when exposed to latex particles coated with IgG. Levels of GPI were decreased experimentally in normal platelets by treating them with chymotrypsin. Platelets treated in this manner did not aggregate or release [14C]serotonin in response to ristocetin-VIII:vWf. They did, however, both aggregate and release when incubated with heat-aggregated IgG, antigen-antibody complexes or latex particles coated with IgG. Thus the presence of GPI is not a prerequisite for platelet stimulation via the Fc receptor.

Topics: Blood Platelets; Chymotrypsin; Electrophoresis, Polyacrylamide Gel; Glycoproteins; Humans; Membrane Proteins; Platelet Aggregation; Platelet Membrane Glycoproteins; Purpura, Thrombocytopenic; Receptors, Fc; Serotonin; Syndrome

In summary: Incubation of platelets with ADP or proteolytic enzymes (chymotrypsin or pronase) results in an exposure of two classes of specific binding sites on platelet surface: low and high affinity fibrinogen receptors. Fibrinogen interaction with these receptors results in platelet aggregation. High affinity fibrinogen receptors are not exposed on thrombasthenic platelets stimulated by ADP but are rendered available on chymotrypsin-treated thrombasthenic platelets; low affinity receptors cannot be exposed by ADP or chymotrypsin on these platelets. Availability of high affinity fibrinogen receptors on thrombasthenic platelets may depend on the residual glycoprotein IIIa. Fibrinogen receptors appear to be associated with glycoproteins IIb, IIIa and a 66,000 Mr platelet membrane component that is exposed during proteolysis of platelet membranes. Some of the platelet-binding sites on the fibrinogen molecule appear to be associated with the COOH-terminal portion of the gamma chain (gamma 374-411). Additional binding sites may also be located in the COOH-terminal portion of the A alpha chain. The conformation of the fibrinogen molecule may be important in its interaction with platelets. Platelet aggregation may result from bridging platelets by fibrinogen molecule in the presence of bivalent cations. In conclusion, platelet interaction with fibrinogen is a complex process involving different binding sites of the fibrinogen molecule. Our own data and review of literature suggest that platelet-interaction with fibrinogen is of major significance in hemostasis.

Topics: Adenosine Diphosphate; Blood Platelets; Cell Membrane; Chymotrypsin; Fibrinogen; Glycoproteins; Humans; Platelet Aggregation; Platelet Membrane Glycoproteins; Purpura, Thrombocytopenic; Receptors, Cell Surface; Structure-Activity Relationship; Syndrome

The 6-h urine recovery of p-aminobenzoic acid (PABA) following the administration of a standard dose of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (BTPABA) was performed in 13 control subjects and two siblings with Shwachman's syndrome. The control subjects showed a recovery of 67 +/- 12.1% (mean +/- 1 SD) of the administered dose, consistent with previously reported values. Unexpectedly, the recovery of PABA in two siblings with Shwachman's syndrome was found to be 67 and 63%, respectively. The values are well within the normal range. In these siblings, fecal chymotrypsin activities were very low when measured with N-acetyl-L-tyrosyl-ethyl ester (ATEE) as substrate, but were normal when BTPABA was the substrate. The duodenal juice of the younger affected child following pancreozymin-secretin stimulation showed very low chymotrypsin activity against ATEE, BTPABA, and N-benzoyl-L-tyrosyl-ethyl ester. These findings suggest that there may be BTPABA-splitting activity in the lower bowel of these siblings with Shwachman's syndrome. This activity might be that of enteric bacteria or of the intestinal mucosa.

Topics: 4-Aminobenzoic Acid; Agranulocytosis; Aminobenzoates; Child; Child, Preschool; Chymotrypsin; Exocrine Pancreatic Insufficiency; Feces; Female; Humans; Infant; Male; Neutropenia; para-Aminobenzoates; Syndrome

Twenty lenses from cataractous eyes have been subjected to enzymatic breakdown by collagenase and alpha-chymotrypsin in order to remove part of the lens capsule and the zonular apparatus. Twelve of the lenses had clinical fibrillopathia epitheliocapsularis (FEC syndrome). In addition four FEC lenses and four ordinary cataractous lenses served as controls. A characteristic fibrillar substance was found in the FEC lenses located to circular epithelium-near areas varying in size from 10 micrometers to 150 micrometers. The circular areas were found in zona germinativa in front of the bow region and corresponded to the discoid plaques of the deep layer. The ultrastructure of the finely fibrillar material of the deep layer were indistinguishable from that of the surface material of the peripheral band and the central disc. A connection between the discoid plaques of deep layer and the peripheral granular band were demonstrated in the form of radial "cobble-stone" sectors seen in partially digested FEC capsules. An increased amount of age dependent spindleshaped formed bodies were also found in FEC lenses. The evidence presented points towards a lenticular origin of the Busacca-bushes in the peripheral ganular band of the lens capsule.

Topics: Aged; Cataract; Chymotrypsin; Eye Diseases; Humans; Lens, Crystalline; Microbial Collagenase; Microscopy, Electron; Middle Aged; Syndrome

The platelet membrane receptor for quinidine- and quinine-dependent antibodies was studied in three patients with the Bernard-Soulier syndrome (BSS) and in normal subjects with immunologic techniques based on the release of 51Cr from labeled platelets. The receptor could not be detected on BSS platelets but was present on platelets from each of 180 normal subjects. BSS platelets reacted normally with other allo- and autoantibodies. In confirmation of previous reports, BSS platelets were found to be deficient in glycoproteins Ib and Is. However, after apparently total cleavage of these proteins from the membrane of normal platelets by controlled hydrolysis with trypsin or chymotrypsin, 80% of the drug-dependent antibody receptor activity was retained. These observations suggest the existence of an additional, hitherto unrecognized membrane defect in Bernard-Soulier platelets.

Topics: Antibodies; Binding Sites; Blood Platelet Disorders; Blood Platelets; Blood Proteins; Cell Membrane; Chymotrypsin; Glycoproteins; Humans; Membrane Proteins; Quinidine; Quinine; Syndrome; Trypsin

In the bronchial mucus of 40 patients with chronic obstructive airway diseases we measured proteolytic activities, the total protein concentrations, alpha1-antitrypsin, alpha1-antichymotrypsin, and the free and bound proteinase inhibitors together with the total proteinase inhibition against trypsin and chymotrypsin. Without exception we always found free proteinase inhibitors together with proteolytic activities. The free-to-bound inhibitor rate was approximately 1:1 alpha1-Antitrypsin and alpha1-antichymotrypsin was measured in sputum only in very low concentrations. One patient with alpha1-anti-trypsin deficiency had no alpha1-antitrypsin, but high concentrations of total proteinase inhibitor-free and bound being in the same relation - in his bronchial mucus. In the alveolar part of the lung, the humoral proteinase inhibitors were effective. In the bronchial part of the lung the specific mucosal inhibitors had the decided importance. The proteinase inhibition of the mucosa-specific inhibitors is probably of great importance for the pathogenesis of airway obstruction, while the humoral proteinase inhibitors are responsible for the pathogenesis of emphysema.

Topics: Adult; Aged; alpha 1-Antitrypsin Deficiency; Bronchitis; Chymotrypsin; Humans; Middle Aged; Mucous Membrane; Mucus; Protease Inhibitors; Proteins; Pulmonary Emphysema; Sputum; Syndrome; Trypsin Inhibitors

Topics: Adult; Age Factors; Aged; Cataract Extraction; Chymotrypsin; Cornea; Edema; Eye Diseases; Female; Humans; Iris; Macula Lutea; Male; Middle Aged; Postoperative Complications; Prednisone; Retinal Diseases; Syndrome; Vitreous Body

Topics: Adrenal Cortex Hormones; Aminopyrine; Asthma; Breathing Exercises; Bronchial Diseases; Chymotrypsin; Deoxyribonuclease I; Drainage; Humans; Oxygen Inhalation Therapy; Posture; Spirometry; Streptodornase and Streptokinase; Streptokinase; Syndrome; Theophylline

Topics: Chymotrypsin; Dehydrocholic Acid; Dyspepsia; Humans; Lipase; Papain; Pepsin A; Piperazines; Syndrome

Topics: Bursitis; Chymotrypsin; Dexamethasone; Diagnosis, Differential; Exercise Therapy; Humans; Hydrocortisone; Periarthritis; Phenylbutazone; Prednisone; Procaine; Shoulder; Shoulder Joint; Shoulder Pain; Syndrome; Therapeutics; Triamcinolone

Topics: Chymotrypsin; Conjunctivitis; Hematologic Tests; Humans; Syndrome