TRANSGLUTAMINASE COVALENTLY INCORPORATES AMINES INTO HUMAN-IMMUNODEFICIENCY-VIRUS ENVELOPE GLYCOPROTEIN GP120 IN-VITRO

Citation
L. Mariniello et al., TRANSGLUTAMINASE COVALENTLY INCORPORATES AMINES INTO HUMAN-IMMUNODEFICIENCY-VIRUS ENVELOPE GLYCOPROTEIN GP120 IN-VITRO, International journal of peptide & protein research, 42(2), 1993, pp. 204-206
Citations number
21
Categorie Soggetti
Biology
ISSN journal
03678377
Volume
42
Issue
2
Year of publication
1993
Pages
204 - 206
Database
ISI
SICI code
0367-8377(1993)42:2<204:TCIAIH>2.0.ZU;2-K
Abstract
Human immunodeficiency virus envelope glycoprotein gp120, but not its precursor gp 160, covalently incorporates both spermidine and glycine ethyl ester in the presence of Ca2+, and transglutaminase purified fro m guinea pig liver. The examined ability to act as enzyme substrate of various glutamine-containing gp120 fragments, including the principal neutralizing determinant, the CD4 binding domain, and the sequence 25 4-274, suggested to be involved in post-binding events and in virus en try in the host cell, indicated the glutamine-265 as possible reactive acyl donor site of the protein. (C) Munksgaard 1993.