Journal ArticleDOI
Acetyl-L-alanyl-L-alanyl-L-alanine methyl ester: a new highly specific elastase substrate.
A Gertler,T Hofmann +1 more
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Acetyl-L-alanine methyl ester is a highly specific esteratic substrate for elastase, and can be used in crude preparations and for the study of proelastase activation.Abstract:
Acetyl-L-alanyl-L-alanyl-L-alanine methyl ester is a highly specific esteratic substrate for elastase. It is only slowly hydrolyzed by trypsin and α-chymotrypsin (0.13 and 1.2%, respectively, of the rate of elastase), and can be used in crude preparations and for the study of proelastase activation. At pH 8.0 and 25°, KM = 0.43 mM; kcat = 73 s−1 and is independent of pH between 7.5 and 10.5. Acetyl-L-alanine methyl ester is a poor substrate with KM 153 mM and kcat 6.7 s−1.read more
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Role of pancreatic proteases in the pathogenesis of ischemic enteropathy.
TL;DR: The effect of various treatments of the intestinal lumen before superior mesenteric artery occlusion was investigated in Wistar rats and total brush border proteins and activities of sucrase, γ-glutamyltransferase, and leucylnapthylamidase in the small bowel decreased.
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Identification of a binary complex of procarboxypeptidase A and a precursor of protease E in porcine pancreatic secretion.
R Kobayashi,Y Kobayashi,C H Hirs +2 more
TL;DR: Porcine protease E has relatively very low activity on intact elastin, but is inert towards acetyl-L-tyrosine ethyl ester and is readily inactivated by diisopropylophosphorofluoridate.
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Proteinase inhibitors in human synovial fluid.
TL;DR: The possibility that enzymatic degradation of articular cartilage is enhanced due to the inactivation of certainproteinase inhibitors, and the possible role of proteinase inhibitors in the pathogenesis of joint diseases are discussed in the light of the reported findings.
Journal ArticleDOI
The trypsin and chymotrypsin inhibitors in chick peas (Cicer arietinum L.). Purification and properties of the inhibitors.
TL;DR: From a crude extract of chick peas (Cicer arietinum L) inhibitors of trypsin and chymotrypsin were isolated by affinity chromatography on a column of TPI-Sepharose 6B.