Limited proteolysis of triose-phosphate isomerase and characterization of the catalytically active peptide complex.
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چکیده
منابع مشابه
The active centre of triose phosphate isomerase.
The molecular weight and amino acid composition of triose phosphate isomerase have been determined. The molecular weight (43000) is lower and the molecular activity (500000) higher than those of most other glycolytic enzymes. Reaction with iodoacetate (studied with radioactive reagent) takes place in two phases: in the first phase, at pH6.3, cysteine and methionine groups react and enzymic acti...
متن کاملCharacterization of Sinorhizobium meliloti triose phosphate isomerase genes.
A Tn5 mutant strain of Sinorhizobium meliloti with an insertion in tpiA (systematic identifier SMc01023), a putative triose phosphate isomerase (TPI)-encoding gene, was isolated. The tpiA mutant grew more slowly than the wild type on rhamnose and did not grow with glycerol as a sole carbon source. The genome of S. meliloti wild-type Rm1021 contains a second predicted TPI-encoding gene, tpiB (SM...
متن کاملsynthesis and characterization of potentially biological active cyclometallated organoplatinum(ii) complexes
this work is presented in five parts. in the first part preparation of the starting complex [pt(c^n)cl(dmso)], 1, in which c^n = n(1),c(2?)-chelated, deprotonated 2-phenylpyridine, and dmso = dimethylsulfoxide, and its reaction with 1 equiv of the biphosphine ligands bis(diphenylphosphino)amine, dppa, or bis(diphenylphosphino)methane, dppm, to give the complex [pt(c^n)cl(dppa)], 2, or [pt(c^n)c...
15 صفحه اولErythrocyte lipids in triose-phosphate isomerase deficiency.
Marked hypoalphalipoproteinemia was found together with relatively low serum cholesterol, triacylglycerol, and LDL levels in a triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1)-deficient Hungarian family, especially in the two compound-heterozygote brothers. Apart from a slight increase in palmitic and stearic acids together with a slight decrease in ole...
متن کاملFolding and association of triose phosphate isomerase from rabbit muscle.
The enzymatic activity and quaternary structure of rabbit muscle triose phosphate isomerase remains unchanged in the concentration range from 2 micrograms/ml to 2 ng/ml. In this concentration range the enzyme can be reactivated after dissociation and denaturation in 6.5 M guanidine hydrochloride. Removal of the denaturant by dilution and separation of inactive wrong aggregates (5-20%) lead back...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)74192-1