Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The relative efficiency of four enzymic-digestion procedures in the release of eight basic drugs from tissue has been studied. Enzymes employed include: subtilisin Carlsberg, trypsin, papain, and neutrase. The results obtained on recovery show that papain digestion gives highest recovery for most of the drugs studied. Papain is suggested as the enzyme of choice. The application of neutrase, a neutral proteinase from B. subtilis, is reported for the first time.
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PMID:Comparative evaluation of some enzymic digestion procedures in the release of basic drugs from tissue. 330 51

Bovine vitreous body and aorta contain extractable leukocyte elastase inhibitors, which were purified by gel filtration and affinity chromatography on agarose-pancreatic elastase. The purified inhibitor preparation from aorta was resolved by polyacrylamide gel electrophoresis into a main band migrating slightly faster than commercial Trasylol and a more weakly stained band migrating close to chymotrypsinogen. The purified inhibitor preparation from both sources inhibited, in a competitive fashion, purified human leukocyte elastase and was ineffective against bovine trypsin and leukocyte cathepsin G or collagenase. These inhibitors from vitreous body and aorta were distinguishable by several criteria from serum inhibitors.
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PMID:Isolation and partial characterization of neutrophil elastase inhibitors from bovine vitreous and aorta. 337 Oct 70

A potent inhibitor of human leukocyte elastase (EC 3.4.21.37) and cathepsin G (EC 3.4.21.20) and of human trypsin (EC 3.4.21.4) has been purified from human parotid secretions. The complete amino acid sequence of this protein has been determined. The sequence suggests that the protein has two domains of about 54 amino acids, each of which contains four disulfide bonds. On the basis of a limited homology to other protease inhibitors, the antielastase and antitrypsin activities are thought to be properties of the C-terminal and N-terminal domains, respectively. The affinity of the inhibitor for leukocyte elastase is very high, suggesting a functional role for the protein in preventing elastase-mediated damage to oral and possibly other mucosal tissues.
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PMID:Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. 346 19

Human lumbar disc tissue when extracted with 4M GuHCl and subjected to dissociative CsCl density gradient ultracentrifugation yielded trypsin inhibitor activity in the low bouyant density fractions (rho less than or equal to 1.38 g/ml). Disc proteoglycans sedimented in the high bouyant density fractions (rho greater than or equal to 1.5 g/ml). Sephadex G75F gel filtration of the low bouyant density protein fractions afforded a major low molecular weight (Kav = 0.5) trypsin inhibitor pool which was further purified by trypsin affinity chromatography. This latter step facilitated separation of the trypsin inhibitors from neutral proteinase activity also present. The trypsin inhibitor fraction so isolated was shown to possess potent inhibitory activity against a range of human serine proteinases including leukocyte elastase and cathepsin G, urokinase, kallikrein, plasmin and thrombin. Significantly this serine proteinase inhibitor preparation effectively prevented degradation of proteoglycans by a neutral proteinase also isolated from the human intervertebral disc.
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PMID:Low molecular weight serine proteinase inhibitors of the human intervertebral disc. 348 24

An inhibitor of serine proteinases from human articular cartilage was purified to homogeneity by sequential ultrafiltration and ion exchange chromatography on CM-Sephadex C-50. The apparent molecular weight of the cationic glycoprotein (pI greater than 10) was determined to be 16.5 X 10(3) by SDS gel electrophoresis. The inhibitor blocked the activity of leukocyte elastase, cathepsin G and trypsin but not leukocyte collagenase. In kinetic studies for the interactions with leukocyte elastase a firm enzyme-inhibitor binding was obtained. Amino acid analyses did not reveal homologies with other serine proteinase inhibitors already purified from human tissues.
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PMID:Purification and characterization of a serine proteinase inhibitor from human articular cartilage. 349 75

We have used a high performance liquid chromatography assay, which detects chymotryptic cleavage of the phe8-his9 bond of angiotensin I to yield angiotensin II, in order to examine human lung mast cells for the presence of chymotryptic activity. Mast cells, purified from human lung by enzymatic dispersion, countercurrent elutriation, and Percoll gradient centrifugation, were lysed or challenged with goat anti-human IgE. In multiple experiments angiotensin II-converting activity was detected in lysates of 10-99% pure mast cell preparations. Regression analysis of net percent release values of histamine and the angiotensin I-converting activity from dose-response experiments demonstrated a correlation between the two parameters, indicating that the chymotrypsin-like enzyme is a constituent of the mast cell secretory granule. The chymotryptic activity was completely inhibited by 10(-3) M phenylmethylsulfonylfluoride but not by 10(-3) M Captopril, and the pH optimum of activity was 7.5-9.5. Gel filtration of released material separated the activity from tryptase and demonstrated an approximate molecular weight of 30-35,000. The mast cell enzyme, like a human skin chymotrypsin-like proteinase, can be distinguished from leukocyte cathepsin G by lack of susceptibility to inhibition by bovine pancreatic trypsin inhibitor. Thus, an enzyme with limited chymotryptic specificity is present in human lung mast cells. The Michaelis constant of the enzyme for angiotensin I of 6.0 X 10(-5) M is similar to that of endothelial cell angiotensin-converting enzyme and is consistent with a reaction of physiologic importance.
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PMID:A human lung mast cell chymotrypsin-like enzyme. Identification and partial characterization. 351 Oct 89

Recent interest in elucidating the role of non-lysosomal proteases in intracellular protein catabolism in muscle has led to various investigations with three alkaline proteases: a trypsin-like, a chymotrypsin-like, and a high molecular weight cysteine proteinase. Although in vitro biochemical assays have revealed the catabolic potential of at least two of these proteases, confirmation of their presence in muscle cells has been difficult. In this study immunohistochemical techniques were employed to localize each of these proteases in rat myoblasts. Antisera against the trypsin-like and chymotrypsin-like proteinase (both serine proteinases) showed strong localization in the cytoplasm immediately around the nucleus. Both also stained chromatin material in the nucleus of these cells. Fluorescent localization of the high molecular weight cysteine proteinase (Proteinase I) also appeared to be cell-associated in the myoblasts. The use of myoblasts in cell culture sections of whole muscle was advantageous, since localization of the proteases could be assessed in the absence of other cell types.
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PMID:Alkaline proteinase localization in myoblasts. 354 Jan 1

Disc tissue consisting of pooled annuli fibrosus and nuclei pulposus from the cadaver of an adolescent aged 19 years was extracted with 4.0 M Gu-HCl. Proteins of low buoyant density (p less than or equal to 1.38 g/ml) containing the disc enzymes and inhibitors were separated from proteoglycans of high buoyant density (p greater than or equal to 1.50 g/ml) by density gradient ultracentrifugation. Sephadex G-75F gel chromatography followed by trypsin affinity chromatography was then used to resolve disc proteolytic and trypsin inhibitory activities. The results obtained were strongly suggestive of the presence of a high molecular weight zymogen which upon activation generated a population of smaller molecular weight proteinases. The disc proteinases obtained by this process showed similar properties in terms of: their pH optima (7.4-7.6); their inhibition patterns by class-specific proteinase inhibitors; their variation of activity as a function of NaCl and lysine concentrations; and the hydrodynamic size of their proteoglycan degradation products. The activated disc neutral proteinase demonstrated many characteristics in common with plasmin; however, unlike the latter, the disc proteinases also showed some calcium dependence.
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PMID:Neutral proteinases of the human intervertebral disc. 354 28

We report the isolation of the human gene encoding an inhibitor of neutrophil elastase and cathepsin G. We have sequenced the gene and a cDNA clone isolated from human parotid tissue. The protein encoded by this gene appears to contain two functional domains, one having a trypsin inhibitory site and the other an elastase inhibitory site. The two-domain structure of the protein is reflected in the organization of the gene, with each domain represented by a separate exon. We have also noted that the intervening sequence separating the trypsin-inhibitor-exon and the elastase-inhibitor-exon is flanked by eleven base-pair direct repeats, suggesting that this intron may have been generated by a transposition-type event.
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PMID:Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases. 364 Mar 38

The major urinary trypsin inhibitor UTI I is a proteoglycan. UTI c (Mr 26,000), produced by chrondroitin lyase digestion of UTI I, was isolated and characterized. About 90% of the glycosaminoglycan chain was removed by this treatment without proteolytic modification, as assessed by amino-acid composition and N-terminal sequence of UTI c. Its electrophoretic mobilities on alkaline and SDS-PAGE are identical with those of UTI II which occurs in urine during storage. To study the role of the glycosaminoglycan chain on the inhibitory properties of UTI I, UTI I and UTI c were compared using different proteinases as target enzymes. The inhibitory activity towards bovine trypsin and chymotrypsin as well as human granulocytic cathepsin G did not differ significantly. However, towards human granulocytic elastase, the equilibrium dissociation constant (Ki) is 5 times higher for UTI c than for UTI I. Weak inhibitory activities were measured on human plasmin, UTI c being more efficient than UTI I. The acid-stability of UTI I is not modified after chrondroitin lyase treatment. UTI I and UTI c are equally sensitive to trypsinolysis indicating that the covalently bound glycosaminoglycan chain does not play an important role for the stability of UTI I.
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PMID:The effect of the glycosaminoglycan chain removal on some properties of the human urinary trypsin inhibitor. 364 44


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