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:3.4.21.1 (chymotrypsin)
10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of the study was to examine the effect of gamma irradiation on the enzymatic as well as the in vivo degradation of polyglycolic acid sutures. The sutures of size 2-0 were irradiated at dosage levels of 0-20 mrad. The three enzymes chosen for this study were esterase, alpha-chymotrypsin, and trypsin. The irradiated sutures were both immersed in the enzyme solutions; their corresponding buffer controls, and implanted in inbred black-and-white hooded hister rats (Liverpool strain). The degradation of PGA sutures was determined mechanically. Among the three enzymes studied, esterase showed the highest enzymatic effect on the degradation of the unirradiated and irradiated PGA sutures. Trypsin's effect on PGA sutures was not observed until 20 mrad. The findings of trypsin demonstrated the hypothesis that synthetic high molecular weight polymers, which are initially resistant to enzymatic degradation, could become prone to enzymatic attack after altering their physical and chemical structures. Implanted PGA sutures maintained a similar or slightly higher mean tensile breaking strength in in vivo degradation compared to in vitro degradation (0.1M tris buffer of pH = 7.5); these degradation profiles suggest that PGA does not display similar behavior in in vivo and in vitro degradations. The magnitude of dissimilarity depends on the radiation dosage and on the duration of degradation, and is speculated to be attributable to the specific action of enzymes with respect to the configuration and chemical structure of the PGA sutures.
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PMID:The effect of gamma irradiation on the enzymatic degradation of polyglycolic acid absorbable sutures. 631 94

One of the esteroproteinases present in the submandibular glands of female mice was purified and characterized. The enzyme, designated proteinase F in this report, had a pI value of 4.6 and a molecular weight of 27600, being comprised of two subunits of 10000 and 18000 daltons. The amino acid composition of proteinase F resembled that of the epidermal growth factor-binding protein, but antiserum against proteinase F only reacted weakly against the binding protein. Proteinase F had an optimum pH at around 9.0 and was strongly inhibited by Cu2+ and Hg2+ (42 and 76% inhibition, respectively, at a concentration of 4 x 10(-6) M). It was also inhibited by aprotinin, phenylmethylsulfonylfluoride, iodoacetamide, leupeptin, antipain, and benzamidine but neither by trypsin inhibitors from pancrease, soybean, or ovomucoid, nor by TLCK, TPCK, and epsilon-amino-n-caproic acid. Although its actual physiological function has yet to be determined, these properties indicate that proteinase F is a new enzyme, being distinguished from known proteinases, kallikrein, plasmin, trypsin, chymotrypsin, tonin, angiotensin-converting enzyme, proteinase A (beta-nerve growth factor endopeptidase), proteinase D (epidermal growth factor-binding protein), P-esterase, renin A, and renin C. Proteinase F was present in the submandibular glands of female mice more abundantly than in those of males, but it increased in males following castration. Thus, proteinase F appears to be affected by male hormones in vivo.
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PMID:A new esteroproteinase (proteinase F) from the submandibular glands of female mice. 633 33

The present work describes the effect of two soya bean protease inhibitors: Kunitz type (SBTI) and Bowman-Birk type (BBTI) on rat trypsin I (TrI), trypsin II (TrII) and chymotrypsin (Chtr) and on human cationic trypsin (hTr). The inhibition spectra show that: (1) SBTI inhibits TrI, TrII, Chtr and hTr esterase activities by 80, 80, 83 and 45%, respectively, at inhibitor-to-enzyme molar ratios of one-to-one, and (2) BBTI inhibits TrI, TrII, Chtr, and hTr esterase activities by 50, 65, 75 and 30%, respectively, at an inhibitor-to-enzyme molar ratio of two-to-one. A similar inhibition pattern was obtained by testing proteolytic activities. It would appear that hTr is less sensitive to soya bean protease inhibitors than each of the rat proteases investigated. This difference in inhibition should be considered when a rat is used as a model to predict the effects of dietary soya bean protease inhibitors on humans.
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PMID:Comparison of the interactions of soya bean protease inhibitors with rat pancreatic enzymes and human trypsin. 661 23

A new substrate, Dns-L-phenylalanine ethyl ester, with high UV absorption has been developed for the determination of the esterase activity of alpha-chymotrypsin and alpha-chymotrypsin-like enzymes. The product, generated by the enzyme action, Dns-L-phenylalanine, was clearly separated from the ester substrate by micro reversed-phase high-performance liquid chromatography. The substrate was highly stable under the enzyme assay conditions used. As little as 0.15 ng of alpha-chymotrypsin and 1.49 ng of subtilisin BPN' could be detected when a long reaction time was employed. Hydrolyses of the substrate by alpha-chymotrypsin and alpha-chymotrypsin-like enzymes were blocked by specific inhibitors of the enzymes.
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PMID:Highly sensitive method for determination of esterase activity of alpha-chymotrypsin and alpha-chymotrypsin-like enzymes using micro high-performance liquid chromatography. 663 Mar 68

Tween 80-hydrolyzing esterases produced by various species of rapidly growing mycobacteria were partially purified from sonicated cell lysates by diethylaminoethyl (DEAE) cellulose and subsequent Sephadex G-150 column chromatographies. The amount of the esterase produced per gram of bacterial cells varied markedly with each species. Mycobacterium smegmatis, M. chelonei, and M. phlei were high producers and M. chitae and M. diernhoferi were low producers of Tween-hydrolyzing esterase. The resistance of each mycobacterial strain to oleic acid correlated well with their esterase-producing ability. All the esterases studied were adsorbed on DEAE cellulose in 50 mM Tris-HCl buffer (pH 7.5), indicating that they are acidic proteins. Esterases of M. smegmatis, M. chitae, M. fortuitum, and M. phlei were eluted from DEAE at high concentrations (0.11-0.18 M) of ammonium sulfate, while those of M. parafortuitum and M. diernhoferi were eluted at lower concentrations (0.05-0.08 M). With Sephadex G-150 gel filtration, all esterases were shown to have similar molecular weights (36,000 to 58,000). On the basis of heat-stability and trypsin- or chymotrypsin-sensitivity, these esterases were divided into three groups: one was heat-stable and protease-sensitive (M. smegmatis and M. fortuitum), another was heat-labile and protease-resistant (M. chelonei), and the other was the intermediate of the above two groups (M. diernhoferi).
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PMID:Physicochemical characterization of Tween 80-hydrolyzing esterases produced by rapidly growing mycobacteria. 664 84

Four 3-alkylthio-1,1,1-trifluoro-2-propanones with juvenile hormone-like side chains were prepared from citronellol and homogeraniol. These substrates were designed as possible transition-state analogs for the juvenile hormone (JH)-specific esterases present in insects. These four isoprenoid trifluormethyl ketones were assayed in vitro with JH esterase and general esterases from larvae of the cabbage looper, Trichoplusia ni (Lepidoptera, Noctuidae), and with eel acetylcholinesterase and bovine chymotrypsin. JH esterase inhibition I50 values were in the nanomolar range for all four compounds, while the other esterases had I50's which were 10(3) to 10(5) higher. The high selectivity of these inhibitors is believed to be due to their similarity in size and functionality to natural JH III. Treatment of T. ni larvae in vivo with solutions of the most active analog, 3-[(E)-4,8-dimethyl-3,7-nonadienylthio]-1,1,1-trifluoro-2-propanon e (DNTFP) causes a dose-dependent delay in pupation and a concurrent selective inhibition of JH esterase. These data support the hypothesis that the reduction in in vivo JH titer in larval T. ni is due, in part, to hydrolysis of the hormone by selective esterases. DNTFP appears to be competing with JH for the active site of JH esterase.
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PMID:Synthesis and bioassay of isoprenoid 3-alkylthio-1,1,1-trifluoro-2-propanones: potent, selective inhibitors of juvenile hormone esterase. 669 51

The collagenolytic serine protease (crab protease) isolated from the hepatopancreas of the fiddler crab, Uca pugilator, has been investigated with respect to its peptide bond specificity and catalytic properties by using noncollagenous substrates. In contrast to vertebrate collagenases, crab protease is a good general protease capable of degrading a variety of polypeptide and synthetic low molecular weight substrates. Crab protease displays a broad range of specificity, cleaving on the carboxyl-terminal side of residues with both positively and negatively charged side chains as well as hydrophobic side chains. The enzyme appears to favor tyrosyl, phenylalanyl, leucyl, and perhaps lysyl residues and, to a lesser extent, arginyl and glutamyl residues. The rate of cleavage of polypeptide substrates is similar to chymotrypsin but is significantly less than trypsin or chymotrypsin for low molecular weight esterase and amidase substrates. Crab protease is effectively inhibited by chymostatin but not by leupeptin or elastatinal. Several common chloromethyl ketone derivatives of phenylalanine and lysine are also ineffective, although crab protease efficiently cleaves at these residues in polypeptide substrates.
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PMID:Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with noncollagenous substrates. 678 31

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

Previous studies demonstrated that proteolytic activity is associated with isolated rabbit sperm nuclei and is responsible for the degradation of nuclear protamine that occurs during thiol-induced in vitro decondensation of the nuclei (Zirkin and Chang, 1977; Chang and Zirkin, 1978). In this study, we present the results of experiments designed to characterize this proteolytic activity. Basic protein isolated from rabbit sperm nuclei incubated with 5 mM dithiothreitol (DTT) and 1 percent Triton X-100 for increasing periods of time exhibited progressively faster migrating bands on acid-urea polyacrylamide gels, reflection the progressive degradation of protamine. Ultimately, a specific and characteristic peptide banding pattern resulted. When sperm nuclei were treated with the esterase inhibitor nitrophenyl-p-guanidino benzoate (NPGB) to inhibit the nuclear-associated proteolytic activity and then incubated with one of several exogenous proteinases in addition to DTT and Triton X-100, characteristic peptide banding patterns were seen for each exogenous proteinase employed. For trypsin, chymotrypsin, pronase, and papain, the peptide banding patterns differed from one another and from the pattern characteristic of protamine degradation by the nuclear-associated proteinase. By contrast, when rabbit acrosin served as the exogenous proteinase, the peptide banding pattern seen was identical to the pattern characteristic of the nuclear-associated proteinase. These results demonstrate directly that the proteinase associated with rabbit sperm nuclei and involved in sperm nuclear decondensation in vitro is acrosinlike.
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PMID:Involvement of an acrosinlike proteinase in the sulfhydryl-induced degradation of rabbit sperm nuclear protamine. 698 41

Two highly purified forms of acid-stable proteinase inhibitor from urine of pregnant women with nephropathies (Mr 22000 and 32000, ASI-22 and ASI-32, respectively) were obtained. The preparations were homogenous in molecular mass and polymorphous in molecular charge (pI from 3.9 to 4.2). ASI-22 an ASI-32 effectively inhibited trypsin and chymotrypsin (Ki approximately 1 x 10(-8)-1 x 10(-9) M, ka approximately 10(5)M-1 sec-1, kd approximately 3 x 10(-4) sec-1) by the permanent mechanism of action. Both forms inhibited the esterase activity of pancreatic pig elastase by the progressive mechanism of action (ki approximately 1 x 10(4)M-1 min-1 at 37 degrees). Rabbit monospecific antiserum to total ASI-22 and ASI-32 preparation was obtained 1 ml of the anti-ASI-serum contained 95 micrograms of antibodies. Total ASI preparations was immunochemically homogenous and had antigenic similarity to inter-alpha-trypsin inhibitor from human plasma.
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PMID:[Acid-stable proteinase inhibitor from the urine of pregnant women, the properties of the highly purified preparation and the isolation of a monospecific antiserum]. 711 61


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