Triose Phosphate Isomerase from Bakers' Yeast
نویسندگان
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 کاملErythrocyte 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...
متن کاملCrystallization of yeast triose phosphate isomerase from polyethylene glycol. Protein crystal formation following phase separation.
A new crystal form of yeast triose phosphate isomerase has been grown from solutions of the enzyme in polyethylene glycol (PEG) of average molecular weight 4000. The crystals are monoclinic, space group P21, with a = 61.3 A, b = 98.4 A, c = 49.7 A, /3 = 90.9”. There is one dimeric molecule per asymmetric unit. Data are observable to at least 1.3A resolution. Crystallization can be achieved afte...
متن کاملThe subunit structure of phosphoglucose isomerase from bakers' yeast.
Bakers' yeast phosphoglucose isomerase was studied by both chemical and physical methods to determine its submit structure. Gel filtration in 6 M guanidine HCl as well as acrylamide gel electrophoresis of sodium dodecyl sulfatedentured phosphoglucose isomerase showed two speices corresponding to one-half and one-fourth of the preparative molecular weight of 119,400 determined by equilibrium cen...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45253-8