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Characterization of specificity of subtilisin Carlsberg towards peptide T by high-performance liquid chromatography and electrospray mass spectrometry.

Abstract：

:Peptide T has a sequence (Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr) belonging to HIV envelope that is involved in the interaction with CD(4) receptor of T lymphocytes. Research of protease activities towards this peptide is very relevant for AIDS therapy. Characterization of specificity of subtilisin Carlsberg towards this very hydrophilic peptide is proposed by using high-performance liquid chromatography and mass spectrometry. Peptide T was totally hydrolysed by the protease after 24 h. Separation of hydrophilic fragments was perfected with an hydrophilic stationary phase and a reversed acetonitrile gradient. Peptide masses were determined by ion spray mass spectrometry. Four primary and one secondary hydrolysis products were found, corresponding to cleavage at the carboxylic side of threonine. Specifities of subtilisin Carlsberg towards the Segments 19 to 26 of bovine pancreatic ribonuclease A, an homologous fragment of peptide T, and peptide T were compared.

journal_name

Enzyme Microb Technol

journal_title

Enzyme and microbial technology

authors

Nedjar-Arroumea N,Paon M,Koralewski F,Friboulet A,Kouach M,Briand G,Leroy Y,Guillochon D

doi

10.1016/s0141-0229(99)00170-2

keywords:

subject

Has Abstract

pub_date

2000-03-01 00:00:00

pages

374-380

issue

5-6

eissn

0141-0229

issn

1879-0909

pii

S0141022999001702

journal_volume

26

pub_type

杂志文章

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