The composition of the rabbit muscle triosephosphate isomerase isozymes of two different subunits

Krietsch, Wolfgang K. G.; Pentchiev, Peter G.; Machleidt, Werner; Klingenburg, Helgard

doi:10.1016/0014-5793(70)80511-7

Cited by 10 publications

(3 citation statements)

References 10 publications

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“…Properties of chicken muscle triose phosphate isomerase The enzyme isolated as described above migrates as a single band on polyacrylamide-gel electrophoresis, in the presence and absence of sodium dodecyl sulphate. The molecular heterogeneity of crystalline isomerase from rabbit muscle (see Norton et al, 1970;Krietsch et al, 1970b) is evidently not apparent with enzyme from chicken breast muscle. This agrees with the distribution of isomerase activity on starch-gel electrophoresis of muscle extracts from different species reported by Scopes (1968).…”

Section: Resultsmentioning

confidence: 99%

Specificity and kinetics of triose phosphate isomerase from chicken muscle

Putman

Coulson

Farley

et al. 1972

Biochemical Journal

109

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The isolation of crystalline triose phosphate isomerase from chicken breast muscle is described. The values of k(cat.) and K(m) for the reaction in each direction were determined from experiments over wide substrate-concentration ranges, and the reactions were shown to obey simple Michaelis-Menten kinetics. With d-glyceraldehyde 3-phosphate as substrate, k(cat.) is 2.56x10(5)min(-1) and K(m) is 0.47mm; with dihydroxyacetone phosphate as substrate, k(cat.) is 2.59x10(4)min(-1) and K(m) is 0.97mm. The enzyme-catalysed exchange of the methyl hydrogen atoms of the ;virtual substrate' monohydroxyacetone phosphate with solvent (2)H(2)O or (3)H(2)O was shown. This exchange is about 10(4)-fold slower than the corresponding exchange of the C-3 hydrogen of dihydroxyacetone phosphate. The other deoxy substrate, 3-hydroxypropionaldehyde phosphate, was synthesized, but is too unstable in aqueous solution for analogous proton-exchange reactions to be studied.

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Section: Resultsmentioning

confidence: 99%

Specificity and kinetics of triose phosphate isomerase from chicken muscle

Putman

Coulson

Farley

et al. 1972

Biochemical Journal

109

View full text Add to dashboard Cite

show abstract

“…Electrophoretic studies on triosephosphate isomerase (D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1 .I ., TPI) have shown in most cases three bands migrating close to one another; such results have been obtained in man [l] , rabbit [ 1,2] and other animals [3]. According to a recent paper by Krietsch et al [4] the intermediary band is the result of hybridization between the two others. Sometimes faster bands have been observed [3] but they are fainter than the three major ones.…”

Section: Introductionmentioning

confidence: 94%

“…According to a recent paper by Krietsch et al [4] the intermediary band is the result of hybridization between the two others. Sometimes faster bands have been observed [3] but they are fainter than the three major ones.…”

Section: Introductionmentioning

confidence: 99%