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The kinetics and thermal stability of phosphogluco‐isomerase isozymes of ryegrasses ( Lolium spp.)
Author(s) -
Jones Thomas W. A.
Publication year - 1985
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1985.tb02311.x
Subject(s) - lolium perenne , lolium , lolium multiflorum , isozyme , biology , allele , kinetics , biochemistry , botany , poaceae , enzyme , gene , physics , quantum mechanics
The Michaelis constants (K m ) and activation energies (E a ) for allozymes of cytosolic phosphogluco‐isomerase (PGI‐2; EC 5.3.1.9) from ryegrasses ( Lolium perenne L., Lolium multiflorum Lam. and interspecific hybrids) have been investigated. Differences were found between the allelic isozymes, but intra‐allelic variations were at least as large. The thermal stability of the isozymes also varied, with the most commonly occurring form (the b ‐allozyme) having the highest stability at 50°C. Some possible explanations for these findings are discussed and the implications for plant breeders outlined.