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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Article . 1988 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
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Immunological properties of rat phosphoglycerate mutase isozymes

Authors: Castellá, Judit; Ureña, Jesús; Ludevid, M. Dolors; Carreras, José; Climent, Fernando;

Immunological properties of rat phosphoglycerate mutase isozymes

Abstract

In mammalian tissues three phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1) isozymes result from the homo-dimeric and hetero-dimeric combinations of two subunits (types M and B). Whereas rabbit antisera against type M subunit (purified from rat muscle) and against type BB isozyme (purified from rat brain) possessed a high degree of specificity, both antisera reacted with type BB and MM isozymes, as demonstrated by immunoneutralization and ELISA. Both the M subunit and B subunit were more immunoreactive than their respective dimeric isozymes. Subunits type M and B may possess common antigenic determinants, and some of these determinants may be sterically hindered in their dimeric structures.

Keywords

Isoenzymes, Molecular Weight, Phosphotransferases, Bisphosphoglycerate Mutase, Animals, Enzyme-Linked Immunosorbent Assay, Rats

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popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
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