| Literature DB >> 3002449 |
H Weingarten, R Martin, J Feder.
Abstract
The active site specificity of vertebrate collagenase was mapped with the synthesis of a variety of peptides, peptolides, and peptide esters. The enzyme was found to prefer very lipophilic sequences, and it was also found to be an esterase. The thio peptolide Ac-Pro-Leu-Gly-SCH[CH2CH(CH3)2]CO-Leu-Gly-OC2H5 was found to be an exceptional substrate. High-performance liquid chromatography and tandem mass spectrometry were used to unambiguously establish the cleavage site in several peptide substrates.Entities:
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Year: 1985 PMID: 3002449 DOI: 10.1021/bi00344a064
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162