Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Gene/Protein
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Target Concepts:
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Enzyme
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Query: EC:3.4.24.3 (
collagenase
)
18,340
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Human tooth slabs were used to observe the effect of several kinds of organic acids and proteolytic enzymes on the production of artificial caries of enamel. Acidic gels were made by formic, acetic and lactic acids separately or in mixed form. The experiments were done in a period of 10 days. After this the specimens were prepared in ground sections and observed under optic microscope. The depth of the artificial lesions was measured by a micrometric scale in the eye lens of the microscope. The enzymes used for investigation were
papain
, trypsin and
collagenase
. The surfaces of the tooth were treated with fresh enzyme solutions every day and then with mixed acid gels. This was done alternately every day in a period of ten days. The results showed that lesions produced by formic acid gel were deeper than those produced by other acids or mixed acid gels. No effect was observed on the depth of the lesion by enzymatic treatments.
...
PMID:[The effect of several acids and proteolytic enzymes on the production of artificial caries]. 209 67
The relationship between the sensitivity (the pD2 value) of carbachol and the density (the total concentration of receptors) of muscarinic receptors using single cells from the guinea pig taenia caecum prepared with a mixture of crude
collagenase
and trypsin inhibitor, purified
collagenase
alone, and a mixture of purified
collagenase
and
papain
was examined. The sensitivity of the single cells prepared with a mixture of purified
collagenase
and
papain
was about 10 times more effective than that of the single cells prepared under other conditions. The dissociation constant of [3H]quinuclidinyl benzilate (QNB) and Hill's coefficient did not change in the single cells prepared under the three conditions, though the maximum binding sites were significantly greater in the cells prepared with the mixture of purified
collagenase
and
papain
than in those prepared by other means. These results suggest that the increase in the sensitivity of carbachol obtained in the single cells prepared with this mixture is due to the increase in the density of muscarinic receptors and also suggest that the effects of this enzyme mixture may be due to an increase in the incorporation of newly synthesized receptors and (or) changes in receptor turnover.
...
PMID:Relationship between sensitivity and density of muscarinic receptors in single smooth muscle cells of guinea pig taenia caecum prepared under three conditions. 216 66
Papain, trypsin and
collagenase
were used in the experiment for the study of their effects on the demineralization of enamel surface by organic acids in vivo. No effect of any of the enzymes was observed. The use of
papain
and trypsin in treating tooth surfaces in vitro, no matter whether sodium bisulfite was used, showed no effect on the demineralization of the enamel by mixed organic acids. But, by the analysis of amino acids in the enzyme solutions before and after treating tooth surface, it was shown that some proteinous substances were destroyed. Accordingly, it can be suggested that the enzyme takes no part in the destruction of the inorganic tooth substance.
...
PMID:[Effects of proteolytic enzymes on demineralization of enamel]. 216 74
Proteoglycans were extracted from nuclease-digested sonicates of 10(9) rat basophilic leukemia (RBL-1) cells by the addition of 0.1% Zwittergent 3-12 and 4 M guanidine hydrochloride and were purified by sequential CsCl density gradient ultracentrifugation, DE52 ion exchange chromatography, and Sepharose CL-6B gel filtration chromatography under dissociative conditions. Between 0.3 and 0.8 mg of purified proteoglycan was obtained from approximately 1 g initial dry weight of cells with a purification of 200-800-fold. The purified proteoglycans had a hydrodynamic size range of Mr 100,000-150,000 and were resistant to degradation by a molar excess of trypsin, alpha-chymotrypsin, Pronase,
papain
, chymopapain,
collagenase
, and elastase. Amino acid analysis of the peptide core revealed a preponderance of Gly (35.4%), Ser (22.5%), and Ala (9.5%). Approximately 70% of the glycosaminoglycan side chains of RBL-1 proteoglycans were digested by chondroitinase ABC and 27% were hydrolyzed by treatment with nitrous acid. Sephadex G-200 chromatography of glycosaminoglycans liberated from the intact molecule by beta-elimination demonstrated that both the nitrous acid-resistant (chondroitin sulfate) and the chondroitinase ABC-resistant (heparin/heparan sulfate) glycosaminoglycans were of approximately Mr 12,000. Analysis of the chondroitin sulfate disaccharides in different preparations by amino-cyano high performance liquid chromatography revealed that 9-29% were the unusual disulfated disaccharide chondroitin sulfate di-B (IdUA-2-SO4----GalNAc-4-SO4); the remainder were the monosulfated disaccharide GlcUA----GalNAc-4-SO4. Subpopulations of proteoglycans in one preparation were separated by anion exchange high performance liquid chromatography and were found to contain chondroitin sulfate glycosaminoglycans whose disulfated disaccharides ranged from 9-49%. However, no segregation of subpopulations without both chondroitin sulfate di-B and heparin/heparan sulfate glycosaminoglycans was achieved, suggesting that RBL-1 proteoglycans might be hybrids containing both classes of glycosaminoglycans. Sepharose CL-6B chromatography of RBL-1 proteoglycans digested with chondroitinase ABC revealed that less than 7% of the molecules in the digest chromatographed with the hydrodynamic size of undigested proteoglycans, suggesting that at most 7% of the proteoglycans lack chondroitin sulfate glycosaminoglycans.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:Purification and characterization of protease-resistant secretory granule proteoglycans containing chondroitin sulfate di-B and heparin-like glycosaminoglycans from rat basophilic leukemia cells. 241 30
To study the properties of vascular smooth muscle in hypertension without the influence of the nerves and endothelium, a procedure was developed to isolate single smooth muscle cells from tail arteries of spontaneously hypertensive rats (SHR) and Wistar-Kyoto (WKY) normotensive control rats. Perfusion of intact arteries with a solution of
papain
and
collagenase
produced dense populations of viable cells (more than 10(4) cells/ml) that remained relaxed in the presence of physiological levels of calcium. Contractile responses of smooth muscle cells from the SHR were significantly more sensitive to noradrenaline, potassium depolarization, and the calcium channel agonist Bay K 8644 compared with those from WKY rats. Enhanced sensitivity to calcium in the SHR was also observed on readdition of calcium to cells preincubated in noradrenaline or KCl in a calcium-free medium. These results provide evidence for alterations in the properties of vascular smooth muscle in the SHR at the single cell level.
...
PMID:Isolation and characterization of single vascular smooth muscle cells from spontaneously hypertensive rats. 247 94
Male, 10-week-old C57B1 10 mice received a single intraarticular injection in the knee joints with
papain
, iodoacetate, or
collagenase
. This led to osteoarthritic lesions, such as matrix depletion, chondrocyte proliferation, and osteophyte formation, in the injected knee joints within several weeks. After injection of iodoacetate and
papain
, the main osteoarthritic alterations were localized in the femoropatellar joint, whereas injection of
collagenase
led to marked osteoarthritic lesions in the femorotibial joint. The mechanism of induction of these alterations appears to differ for iodoacetate and
papain
on one site and
collagenase
on the other site. Data are presented that
collagenase
injection, by way of damaging ligaments and tendons, destabilizes the knee joint eventually leading to osteoarthritic alterations. In contrast, injection of
papain
or iodoacetate directly interferes with cartilage metabolism resulting in osteoarthritic changes.
...
PMID:Development of osteoarthritic lesions in mice by "metabolic" and "mechanical" alterations in the knee joints. 255 24
Commercial Collagenase* prepared from Clostridium histolyticum is widely used in isolation of pancreatic islets. It is known that the enzyme is very impure and that there are substantial variations in effectiveness between batches. Our studies suggest that one of the impurities of importance in islet isolation is a protease that has not been very well characterized. Comparison of two batches of enzyme, one of which was known to give good yields of islets and the other poor yields, showed that they had very similar activity against collagen (measured by digestion of insoluble collagen followed by assay of soluble products with ninhydrin) but substantially different activities against azocasein as measured by optical density increase (measured by release of dye). Eighteen batches of Collagenase were examined for efficiency in islet isolation, and the yields obtained correlated with manufacturer's data of activity against casein. The data show that low caseinase activity is associated with performance in islet isolation (r = .5 after adjusting for
collagenase
activity). The effect of supplementing a batch of
collagenase
, known to be poor in isolating islets, with proteolytic enzymes was investigated. Trypsin and
papain
had apparently no effect, but dispase significantly increased yield. Dispase alone failed to digest pancreas. Size-exclusion high-performance liquid chromatography identified a peak associated with high protease activity and efficiency in islet isolation, having an Mr of approximately 30,000, compared to 78,000 for
collagenase
. The protease, like
collagenase
, is inhibited by EDTA. Increased Ca2+ and Mg2+ (up to 10 mM) did not affect activity. Both the protease and
collagenase
are stable under normal use but are inactivated by heating at 56 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Protease activity in pancreatic islet isolation by enzymatic digestion. 264 34
The chemical nature of anionic sites located on both fronts of the endothelial cells (ECs) and in the basement membrane (BM) of mouse brain capillaries was studied using tissue sections embedded in Lowicryl K4M and cationic colloidal gold. Before labelling with cationic probe, the sections were digested with the following enzymes: trypsin,
papain
, pronase E, proteinase K,
collagenase
, chondroitinase ABC, hyaluronidase, heparinase, heparitinase, neuraminidase and endoglycosidase H. The results indicate that the negatively charged surface layer on the luminal front differs in chemical nature from that on the abluminal front of the EC. Anionic sites located on the luminal surface of the plasmalemma of the ECs are mainly contributed by sialic acid residues of acidic glycoproteins. On the contrary, the anionic domains on the abluminal front of the EC represent mixed proteoglycan and acid glycopeptides containing hydrophobic amino acids, sialic acid residues, and are rich in heparan sulphate-bearing glycosaminoglycans. The anionic sites of the BM are contributed in a substantial degree by chondroitin and heparan sulphate-rich glycosaminoglycans. The effect of endoglycosidase H suggests that glycopeptides containing oligomannosyl residues linked to N-acetylglucosamine contribute in small degree in maintenance of the negative charge in the BM, but not on the surfaces of the EC. These results show that brain endothelium bears surface anionic domains differing chemically from those described for some fenestrated and continuous endothelia. The distribution of anionic sites indicates that the discrimination against various negatively charged molecules takes place on both fronts of the ECs as well as in the BM of brain micro-blood vessels. The exact role of these domains in the function of the blood-brain barrier remains to be established.
...
PMID:Ultracytochemical characterization of anionic sites in the wall of brain capillaries. 274 7
Procedures for isolating single smooth muscle cells from tenia coli of guinea pigs have been developed. The cells were isolated with a combination of highly purified
collagenase
and a small amount of strong peptidase,
papain
, in the presence of Ca. This combination resulted in approximately a 100-fold yield of the single cells as compared with the ordinary method in which only
collagenase
preparations contaminated with various peptidases were used. More than 95% of the single cells were viable when examined by the trypan blue exclusion technique. In addition, this combination greatly increased the responsiveness to agonists such as carbachol (CCh). A concentration of CCh for the half maximum response for this preparation was about one five-hundredth that of cells prepared by the ordinary method. This value was approximately one-quarter that of intact tissue. This preparation can be used to investigate the physiology, pharmacology, and biochemistry of smooth muscle.
...
PMID:Improvement of a procedure for preparing single smooth muscle cells from guinea pig tenia coli by purified collagenase and papain. 283 8
Hedgehog plasma was separated by gel filtration on Sephacryl S-200, the fractions resolved by electrophoresis and the electrophoretograms characterized for
collagenase
,
papain
and plasmin inhibiting activities with the high mol. wt substrate casein. The three inhibitors previously identified as alpha 2-, alpha 2-beta- and beta-macroglobulins were found to inhibit all three proteases. These were the only
collagenase
inhibitors found in plasma. Hedgehog alpha 2-chymotrypsin inhibitor and beta-protease inhibitor were both found to also inhibit
papain
. Three new inhibitors specific for
papain
(gamma-, alpha 2- and alpha 1-cysteine protease inhibitors) and one for plasmin (alpha 2-antiplasmin) were also found, bringing the number of protease inhibitors in hedgehog plasma to 14. Immunological cross-reactivity as studied by immunoelectrophoresis showed homology between hedgehog alpha 2-macroglobulin and rat murinoglobulin I and between hedgehog alpha 2-antithrombin and rat antithrombin III.
...
PMID:Further studies of plasma protease inhibitors in the hedgehog, Erinaceus europaeus; collagenase, papain and plasmin inhibitors. 288 40
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