NDLI: Conversion of inactive glycosylation inhibiting factor to bioactive derivatives by modification of a SH group.

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Conversion of inactive glycosylation inhibiting factor to bioactive derivatives by modification of a SH group.

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Conversion of inactive glycosylation inhibiting factor to bioactive derivatives by modification of a SH group.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Oyama, Y. Liu, Y. C. Watarai, H. Nakano, T. Mikayama, T. Ishizaka, K.
Description	Author Affiliation: Nakano T ( La Jolla Institute for Allergy and Immunology, CA 92037, USA.);
Abstract	Escherichia coli-derived recombinant human glycosylation inhibiting factor (rhGIF) contains three cysteine residues (Cys-57, -60, and -81). All SH groups in the cysteine residues are free, and the GIF molecule had no biologic activity. Carboxymethylation of the SH group of Cys-60 in the molecule resulted in the generation of bioactivity, although the activity of the carboxymethylated GIF was 10- to 20-fold less than that of suppressor T cell (Ts)-derived GIF. However, treatment of the inactive rhGIF with ethylmercurithiosalicylate or 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) resulted in the generation of derivatives whose bioactivity was comparable to that of the Ts-derived bioactive GIF. The activity of these derivatives was lost by treatment with DTT. Isolation and chemical analysis of the DTNB-treated GIF derivative revealed that binding the 5-thio-2-nitrobenzoic acid group with Cys-60 was responsible for the generation of the highly bioactive derivative. Inactive cytosolic GIF from mammalian cells could also be converted to bioactive derivative by treatment with the SH reagent, while Ts-derived bioactive GIF was inactivated by DTT. These results, together with an x-ray crystal structure of GIF molecules, strongly suggest that the generation of bioactivity of GIF in Ts cells is due to posttranslational modifications that result in conformational changes in the molecule.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Lymphokines Chemistry Pharmacology Prostatic Secretory Proteins Amino Acid Sequence Biological Assay Disulfides Enzyme-Linked Immunosorbent Assay Escherichia Coli Genetics Glycosylation Drug Effects Mass Spectrometry Molecular Sequence Data Peptide Mapping Protein Conformation Recombinant Proteins Sulfhydryl Reagents Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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