ISSN:
1573-4927
Keywords:
phosphoglycerate kinase-1
;
mouse
;
allozymes
;
properties
;
antibody
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The two allelic isozymes (wild-type 1B and the electrophoretic variant 1A) of mouse X-linked phosphoglycerate kinase (PGK-1) have been purified by affinity chromatography. The following properties were determined for both forms: molecular weight, specific activity, nucleotide specificity, K m values of the four substrates, K i of the ATP-ribosyladipoyldihydrazo-Mg complex, turnover number, activation energy, pH and ionic strength dependence, thermostability, content of free sulfhydryl groups, and antibody cross-reactivity. With the exception of specific activity and thermostability, both allozymes appear to be identical in all properties. The higher in vitro specific activity of the 1B allozyme may be due to the higher thermostability. No antigenic difference could be detected between the two allozymes.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00484441
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