Z-苯丙胺酰-精氨酸-7-氨基-4-甲基香豆素盐酸盐
Z-苯丙胺酰-精氨酸-7-氨基-4-甲基香豆素盐酸盐结构式
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常用名 | Z-苯丙胺酰-精氨酸-7-氨基-4-甲基香豆素盐酸盐 | 英文名 | Z-Phe-Arg-AMC · HCl |
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| CAS号 | 65147-22-0 | 分子量 | 612.68 | |
| 密度 | 1.32 g/cm3 | 沸点 | N/A | |
| 分子式 | C33H36N6O6 | 熔点 | N/A | |
| MSDS | 美版 | 闪点 | N/A |
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Assay of coagulation proteases using peptide chromogenic and fluorogenic substrates.
Meth. Enzymol. 80 , 341, (1981)
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Residue-specific annotation of disorder-to-order transition and cathepsin inhibition of a propeptide-like crammer from D. melanogaster.
PLoS ONE 8(1) , e54187, (2013) Drosophila melanogaster crammer is a novel cathepsin inhibitor involved in long-term memory formation. A molten globule-to-ordered structure transition is required for cathepsin inhibition. This study reports the use of alanine scanning to probe the critical ... |
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Production of anti-peptide antibodies against trypanopain-Tb from Trypanosoma brucei brucei: effects of antibodies on enzyme activity against Z-Phe-Arg-AMC.
Immunopharmacology 36(2-3) , 295-303, (1997) Anti-peptide antibodies were produced against the cysteine proteinase trypanopain-Tb from Trypanosoma brucei brucei and the effects of these antibodies on enzyme activity against carboxybenzoyl (Z)-Phe-Arg-aminomethylcoumarin (AMC) investigated. A peptide was... |
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Modulation of the catalytic activity of cruzipain, the major cysteine proteinase from Trypanosoma cruzi, by temperature and pH.
Eur. J. Biochem. 268(11) , 3253-8, (2001) Cysteine proteinases are relevant to several aspects of the parasite life cycle and of parasite-host relationships. Here, a quantitative investigation of the effect of temperature and pH on the total substrate inhibition of cruzipain, the major papain-like cy... |
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Delineating functionally important regions and residues in the cathepsin B propeptide for inhibitory activity.
FEBS Lett. 393(1) , 24-6, (1996) Synthetic peptides derived from the proregion of rat cathepsin B were used to identify functionally important regions and residues for cathepsin B inhibition. Successive 5 amino acid deletions of a 56 amino acid propeptide from both the N- and C-termini has a... |
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Trypanosomatid cysteine protease activity may be enhanced by a kininogen-like moiety from host serum.
Biochem. J. 305 ( Pt 2) , 549-56, (1995) African trypanosomes contain cysteine proteases (trypanopains) the activity of which can be measured by in vitro digestion of fibrinogen, after electrophoresis in fibrinogen-containing SDS/polyacrylamide gels. When assessed by this procedure, trypanopain from... |
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Interplay between acid phosphatase and cysteine proteases in mediating vitellin degradation during early embryogenesis of Periplaneta americana.
J. Insect Physiol. 54(5) , 883-91, (2008) In this work, we characterized the activities of two classes of proteases and AcP during early embryogenesis of Periplaneta americana. AcP activity was first detected at day 6 and reached a maximum level at day 10 of development. Using phosphoamino acids, pho... |
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The N-terminal part of recombinant human tear lipocalin/von Ebner's gland protein confers cysteine proteinase inhibition depending on the presence of the entire cystatin-like sequence motifs.
Biol. Chem. 382(10) , 1515-20, (2001) Human Tear Lipocalin/von Ebner's gland protein (TL) is a member of the lipocalin superfamily. The protein is secreted by a number of serous glands and tissues and is overproduced under conditions of stress, infection and inflammation. In addition to its typic... |
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Differences in cysteine protease activity in Schistosoma mansoni-resistant and -susceptible Biomphalaria glabrata and characterization of the hepatopancreas cathepsin B Full-length cDNA.
J. Parasitol. 94(3) , 659-68, (2008) Biomphalaria glabrata snails are known to display a wide range of susceptibility phenotypes to Schistosoma mansoni infection depending on the genetics of both the snail and the invading parasite. Evidence exists for a role of hydrolytic enzymes in the defense... |
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Expression in Escherichia coli, refolding, and purification of human procathepsin K, an osteoclast-specific protease.
Protein Expr. Purif. 15(2) , 213-20, (1999) We have constructed and optimized a high yielding Escherichia coli expression system to produce glycosylation-free human procathepsin K and have developed conditions for refolding this enzyme. Recombinant human procathepsin K (EC 3.4.22.38) was expressed in E... |