First determination of the isozyme patterns of phosphoglycerate mutases (E.C. 2.7.5.3) and phosphoglycerate kinases (E.C. 2.7.2.3) in human tissues
β Scribed by R. A. Kamel; K. Berg; F. Schwarzfischer; H. Wischerath
- Publisher
- Springer
- Year
- 1975
- Tongue
- English
- Weight
- 154 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0340-6717
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β¦ Synopsis
We present in this paper the first report about identification of several fractions of phosphoglycerate mutase (PGlyM) activity using starch gel electrophoresis and two different buffer systems. A typical muscle form of PGlyM was detected. It is also shown that isozymes of phosphoglycerate kinase (PGK) can be separated through the buffer system used by Spencer et al; (1964) for the phosphogluco mutase.
π SIMILAR VOLUMES
The polymorphism of the human phosphoglucomutase isozyme PGM3 can be demonstrated in erythrocyte hemolysates by means of horizontal starch gel electrophoresis. Gene frequencies from southwestern Germany are given. The frequency of the allel PGM-23 was estimated to be 0.232.
The reaction of 2,6-diarylidenecyclohexanones with hydrazine hydrate in glacial acetic acid resulted in the formation of diastereomers of (E)-2-acetyl-3-aryl-7-arylidene-3,3a,4,5,6,7-hexahydroindazoles. The relative conΓgurations of these diastereomers were unambiguously assigned using 1H and 13C NM