Limited Proteolysis of Yeast Phosphofructokinase by Subtilisin. Alterations in Enzyme Activity, Subunit Composition, and Hydrodynamic Properties
نویسندگان
چکیده
منابع مشابه
Mutations in the regulatory subunit of soluble phosphofructokinase from yeast.
Mutant alleles of the gene PFK2 have been obtained that alter the sensitivity to ATP inhibition of the soluble yeast phosphofructokinase. One of the alleles makes the enzyme sensitive to micromolar concentrations of ATP. Intragenic revertants of PFK2 mutants confirm that the PFK2 gene determines not only the regulatory properties of the soluble enzyme but also the catalytic activity of particul...
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The incubation of maize malic enzyme at 37 degrees C with trypsin at a ratio of 150:1 of malic enzyme to trypsin caused rapid and complete inactivation of enzyme activity. The inactivation was caused by fairly specific cleavage of the enzyme monomer (62 kDa) into 40 kDa and 20 kDa fragments. The intensity of 40 kDa band increased with the time of treatment of enzyme with trypsin from 2 to 30 mi...
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In this study, we investigated the alterations in the activity, subunit profile, and kinetic regulatory properties of phosphofructokinase (PFK) from human gliomas compared with those from normal human brain. Gliomas showed a decrease in the enzyme activity as compared to normal brain. This decrease in PFK activity was accompanied by a relative increase in the expression of the liver type subuni...
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15 صفحه اولLimited proteolysis by trypsin influences activity of maize phosphoenolpyruvate carboxylase.
Maize phosphoenolpyruvate carboxylase (PEPC) was rapidly and completely inactivated by very low concentrations of trypsin at 37 degrees C. PEP+Mg2+ and several other effectors of PEP carboxylase offered substantial protection against trypsin inactivation. Inactivation resulted from a fairly specific cleavage of 20 kDa peptide from the enzyme subunit. Limited proteolysis under catalytic conditio...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1975
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1975.tb02458.x