alpha-chymotrypsin and Infections

alpha-chymotrypsin has been researched along with Infections* in 10 studies

Reviews

1 review(s) available for alpha-chymotrypsin and Infections

ArticleYear
[Relation between acute phase proteins and body defense: application to the monitoring of infectious states].
    Annales de biologie clinique, 1984, Volume: 42, Issue:1

    All acute and/or chronic pathological processes resulting in tissue damage and destruction lead to an inflammatory response. The purpose of this response is homeostatic and is made up of local and systemic events, the signs of which, taken as a whole, constitute the acute phase syndrome. Among the metabolic changes occurring in this syndrome, the rise in the plasma concentration of a group of heterogenous proteins known as the "Acute Phase Reactant Proteins" ( APRP ) is a very reliable and sensitive indicator of the presence of pathology. Most of these proteins are involved in the mechanisms initiating and controlling the inflammatory response. Some of them seem to establish a link between the body's specific and non-specific defence mechanisms. APRP are indicators of the inflammatory response without being specific to a particular etiology. The degree of variation in APRP levels is not generally speaking a good indicator of the severity or spread of the tissue lesions. On the other hand, they are very useful for detecting and monitoring infectious and/or inflammatory states, whether these are being treated or not. Thus during anti-infectious or anti-inflammatory treatment the return of APRP levels to their physiological baseline is a very good argument in favour of the efficacy of such treatment.

    Topics: Acute-Phase Proteins; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Animals; Blood Proteins; C-Reactive Protein; Ceruloplasmin; Chymotrypsin; Complement C3; Haptoglobins; Humans; Immune Tolerance; Infections; Inflammation; Orosomucoid; Serum Amyloid A Protein

1984

Other Studies

9 other study(ies) available for alpha-chymotrypsin and Infections

ArticleYear
Plasma proteins immunologically related to inter-alpha-trypsin inhibitor.
    Biochimica et biophysica acta, 1988, Apr-14, Volume: 953, Issue:3

    SDS-polyacrylamide gel electrophoresis and immunoblot were applied to analysis of plasma proteins immunologically related to inter-alpha-trypsin inhibitor (ITI). In this system, anti-ITI sera were able to identify ITI and other components with an Mr near 120 kDa which would be degradation products of ITI by limited proteolysis. An anti-UTI (urinary trypsin-inhibitor) serum could detect, beside these derivatives, two minor components (Mr values near 90 and 60 kDa). Analysis of perchloric acid supernatants of plasma samples, using the same technic, induced visualization of a new component, similar to urinary trypsin inhibitor which could not be detected by direct analysis. This one was also characterized in a higher content in pathological samples (renal failure and infectious diseases).

    Topics: Alpha-Globulins; Blood Proteins; Chymotrypsin; Electrophoresis, Polyacrylamide Gel; Glycoproteins; Humans; Immune Sera; Immunoenzyme Techniques; Infections; Kidney Diseases; Trypsin Inhibitors

1988
Elevated titers of serum agglutinators. A serologic indicator of infection.
    American journal of clinical pathology, 1975, Volume: 63, Issue:1

    Elevated titers of serum agglutinators (anti-FabIgG) are associated with significant and severe suppurative infection. Immunosuppression and long-term antibiotic therapy, however, may lead to negative tests.

    Topics: Anti-Bacterial Agents; Antibodies, Anti-Idiotypic; Blood Protein Electrophoresis; Chromatography, DEAE-Cellulose; Chymotrypsin; Coombs Test; Hemagglutination; Humans; Immunoglobulin Fab Fragments; Immunoglobulin Fc Fragments; Immunoglobulin G; Immunosuppression Therapy; Infections; Isoantibodies; Papain; Retrospective Studies; Rh-Hr Blood-Group System; Rheumatoid Factor; Subtilisins; Trypsin

1975
[Enzymatic-antibiotic combination in odontology. 1st observations].
    Hospital (Rio de Janeiro, Brazil), 1970, Volume: 77, Issue:2

    Topics: Anti-Inflammatory Agents; Chymotrypsin; Humans; Infections; Mouth Diseases; Postoperative Complications; Tetracycline; Trypsin

1970
[Enzyme therapy as a physiologically based method of treating acute suppurative diseases of the soft tissues].
    Vestnik khirurgii imeni I. I. Grekova, 1969, Volume: 103, Issue:8

    Topics: Abscess; Acute Disease; Carbuncle; Cellulitis; Chymotrypsin; Deoxyribonucleases; Female; Furunculosis; Humans; Infections; Lymphadenitis; Mastitis; Paronychia; Peptide Hydrolases; Pregnancy; Proctitis; Streptokinase; Suppuration; Surgical Wound Infection; Trypsin

1969
[Combination of tetracycline and pancreatic proteolytic enzymes in the therapy of gynecologic inflammation].
    Praxis, 1969, Apr-29, Volume: 58, Issue:17

    Topics: Adult; Chymotrypsin; Drug Synergism; Female; Genital Diseases, Female; Humans; Infections; Middle Aged; Tetracycline; Trypsin

1969
[THE TETRACYCLINE HC1, TRYPSIN AND CHYMOTRYPSIN COMBINATION: CHYMOCYCLINE].
    Strasbourg medical, 1964, Volume: 15

    Topics: Anti-Bacterial Agents; Chymotrypsin; Hematologic Tests; Humans; Infections; Protein Synthesis Inhibitors; Tetracycline; Trypsin

1964
[A NEW OUTLOOK IN ANTIBACTERIAL THERAPEUTICS. COMBINED USE OF PROTEOLYTIC ANZYMES AND BROAD-SPECTRUM ANTIBIOTICS].
    Medicina, 1964, Sep-25, Volume: 44

    Topics: Anti-Bacterial Agents; Antibiotics, Antitubercular; Chymotrypsin; Drug Therapy; Humans; Hydrolases; Infections; Inflammation; Pharmacology; Protein Synthesis Inhibitors; Tetracycline; Trypsin

1964
[CHYMORAL. CLINICAL ANALYSIS OF ITS THERAPEUTIC POSSIBILITIES].
    Strasbourg medical, 1963, Volume: 14

    Topics: Chymotrypsin; Drug Combinations; Hematologic Tests; Humans; Infections; Surgery, Oral; Trypsin

1963
Pharmacologically active peptides in the blood and urine of animals infected with Babesia rodhaini and other pathogenic organisms.
    British journal of pharmacology and chemotherapy, 1960, Volume: 15

    The blood and urine of mice and rats infected with Babesia rodhaini contain substances which stimulate the isolated guinea-pig ileum and rat duodenum. The amount of active material excreted increases as the infection increases. The active substances are stable to boiling with hydrochloric acid but not with alkali; they pass through a cellophane membrane and are soluble in hot ethanol. They are destroyed rapidly by papain and less rapidly by chymotrypsin, but are unaffected by trypsin or pepsin. Their action on smooth muscle is not affected by atropine, eserine, antihistamines, iproniazid, bretylium or by lysergic acid diethylamide. The active substances are probably peptides and there is evidence that the urine contains a mixture of peptides, some of which relax and some of which contract the rat duodenum. Similar active peptides appear in the urine of mice infected with Plasmodium berghei, Trypanosoma rhodesiense, Streptococcus pyogenes and Rift Valley fever virus.

    Topics: Animals; Atropine; Babesia; Body Fluids; Chymotrypsin; Guinea Pigs; Ileum; Infections; Mice; Muscle, Smooth; Papain; Pepsin A; Peptides; Rats; Trypsin

1960