Journal article
Haptoglobin. A novel mode of biosynthesis of a liver secretory glycoprotein
The Journal of biological chemistry, Vol.256(3), pp.1055-1057
02/10/1981
DOI: 10.1016/S0021-9258(19)69917-5
PMID: 7451486
Abstract
The de novo biosynthesis of the heterotetrameric (alpha 2 beta 2) serum glycoprotein, haptoglobin, was studied using a rabbit reticulocyte cell-free translation system and mRNA preparations from the livers of turpentine-treated rats. Analysis of the translation mixtures with either antisera specific for the alpha-subunit (anti-alpha-IgG) or the beta-subunit (anti-beta-IgG) or the native haptoglobin tetramer (anti-alpha 2 beta 2-IgG) resulted in each instance in the recovery of a single protein exhibiting a Mr = approximately 38,000. Cleavage of the translation product with cyanogen bromide or trypsin resulted in the generation of small peptide fragments that were specifically immunoadsorbed with either anti-alpha-IgG or anti-beta-IgG. These results indicated that the primary translation product of haptoglobin mRNA is a single polypeptide that contains the elements of both the alpha-subunit and the beta-subunit of the protein. Presumably haptoglobin is synthesized in vitro as a single precursor protein that is proteolytically processed post-translationally to form the dissimilar alpha- and beta-subunits of the native protein.
Details
- Title: Subtitle
- Haptoglobin. A novel mode of biosynthesis of a liver secretory glycoprotein
- Creators
- Thomas H HaugenJoan M HanleyEdward C Heath
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.256(3), pp.1055-1057
- DOI
- 10.1016/S0021-9258(19)69917-5
- PMID
- 7451486
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- United States
- Grant note
- AM-19850 / NIADDK NIH HHS
- Language
- English
- Date published
- 02/10/1981
- Academic Unit
- Pathology
- Record Identifier
- 9984047994002771
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