A unique electrophoretic pattern of triosephosphate isomerase in human cultured fibroblasts

Rubinson, Henriette; Vodovar, M; Meienhofer, Marie-Claire; Dreyfus, Jean‐Claude

doi:10.1016/0014-5793(71)80243-0

Cited by 21 publications

(10 citation statements)

References 4 publications

(3 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The a, b and c isozymes were detected in most tissues and probably correspond with the three main isozymes described in previous studies with crude haemolysates and post-mortem tissue extracts (Kaplan et al 1968;Rubinson et al 1971) and with purified red cell TPI (Rozacky et al 1971)) though in the latter study separation was obtained by isoelectric focussing. Components similar to a-c have also been demonstrated by protein staining, after polyacrylamide gel electrophoresis, in purified preparations of human liver TPI (Lee et al 1971).…”

Section: Discussionsupporting

confidence: 80%

See 1 more Smart Citation

Genetic and non‐genetic variation of triose phosphate isomerase isozymes in human tissues

Peters

Hopkinson

Harris

1973

Annals of Human Genetics

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 80%

“…Isozyme i possibly corresponds with the weak very fast (VF) zone described by Rubinson et al (1971). However, it is difficult to be sure about this since the VP zone was observed by Rubinson et al in extracts of cultured fibroblasts but not in skeletal muscle.…”

Section: Variation Of Tpi Isozymes In Human Tissuesmentioning

confidence: 92%

Genetic and non‐genetic variation of triose phosphate isomerase isozymes in human tissues

Peters

Hopkinson

Harris

1973

Annals of Human Genetics

View full text Add to dashboard Cite

“…The weakly stained protein band having the fastest mobility also is believed to have isomerase activity although the close proximity of this band to the major bands precluded a conclusive determination of activity. Such a pattern also was observed by Rubinson et al with human erythrocyte triose-phosphate isomerase [15]. The Sigma rabbit muscle triose-phosphate isomerase had only one protein band associated with isomerase activity (Fig.…”

Section: Electrophoretic Studiessupporting

confidence: 57%

Identification and Characterization of Pituitary Triose‐Phosphate Isomerase

Greenberg

Yen

Bobbitt

1972

European Journal of Biochemistry

View full text Add to dashboard Cite

Several pituitary preparations from various species, including two purzed follicle-stimulating hormone preparations, inhibited the ~-glyceraldehyde-3-phosphate dehydrogenase reaction. The active factor in those preparations that caused the apparent inhibition has been identified as an enzyme, triose phosphate isomerase. Using ~-glyceraldehyde-3-phosphate as the substrate, the optimum pH for the isomerization reaction is 8.4. The partially purified enzyme has a specific activity of 34 pmol dihydroxyacetone phosphate isomerized x min-* x mg protein+. The Km of the enzyme for D-glyceraldehyde 3-phosphate is 0.79 mM, and the K m for dihydroxyacetone phosphate is 1.53 mM. Half of the enzyme activity is lost in 7 min at 55 "C. The molecular weight of the enzyme is estimated to be 56000. The electrophoretic mobility of the enzyme differs from tha.t of the muscle enzyme supplied by Sigma indicating a difference in amino acid composition between the two enzymes. Electrophoresis revealed the presence of two to three isozymes of the pituitary triose phosphate isomerase.Two preparations of follicle-stimulating hormone, supplied by The National Institute of Arthritis and Metabolic Disease, inhibited the reaction of D-glyceraldehyde-3-phosphate dehydrogenase using glyceraldehyde-3-phosphate as the substrate [l]. These two preparations were of ovine (lot #S-4) and porcine (lot # P-1) origin. Another ovine preparation (lot #S-7) did not inhibit this reaction [l]. We thus concluded that the inhibitor was not follicle-stimulating hormone but a contaminant [l]. We also concluded that the inhibitor was not one of the known pituitary hormones we had tested, since none of them inhibited the ~-glyceraldehyde-3-phosphate dehydrogenase reaction El].Bornstein and his associates have reported the isolation of a factor, InG, from a pH-2 hydrolyzate of ovine growth hormone that inhibited D-glyceraldehyde-3-phosphate dehydrogenase and possessed other biological properties [2,3]. The amino acid sequence at both the amino terminal and carboxyl terminal of InG suggested that InG was a peptide from growth hormone that consisted of residues 164 to 188 [4]. A peptide synthesized according to the proposed amino acid sequence of InG had all the biological activities of the isolated InG [a].

show abstract

“…Dreyfus and co-workers have also identified electrophoretically distinct isozymes in human fibroblasts (Rubinson et al, 1971) and have reported that these isozymes are detectable only in fibroblasts derived from hominoid species (Rubinson et al, 1973). Although these isozymes were initially proposed to be the product of a second structural locus (Kester et al, 1977;Yuan et al, 1979), subsequent genetic studies have demonstrated that the constitutive isozyme (TPI-1 subunit) and the thermolabile, cell divisionassociated isozyme (TPI-2 subunit) are actually products of the same structural locus (Decker and Mohrenweiser, 1981).…”

Section: Introductionmentioning

confidence: 99%

Cell proliferation-associated expression of a recently evolved isozyme of triosephosphate isomerase

Decker

Mohrenweiser

1985

Biochem Genet

View full text Add to dashboard Cite

A unique electrophoretic pattern of triosephosphate isomerase in human cultured fibroblasts

Cited by 21 publications

References 4 publications

Genetic and non‐genetic variation of triose phosphate isomerase isozymes in human tissues

Genetic and non‐genetic variation of triose phosphate isomerase isozymes in human tissues

Identification and Characterization of Pituitary Triose‐Phosphate Isomerase

Cell proliferation-associated expression of a recently evolved isozyme of triosephosphate isomerase

Contact Info

Product

Resources

About