Studies on Human Triosephosphate Isomerase
نویسندگان
چکیده
منابع مشابه
Primary structure of human triosephosphate isomerase.
Human placental triosephosphate isomerase was isolated by an improved procedure and recovered with the highest specific activity ever reported. Employing this purification procedure, sufficient amounts of the enzyme were obtained for detailed primary structural studies. For sequences analysis, the enzyme was reduced and carboxymethylated and subjected to tryptic and chymotryptic digestions. The...
متن کاملDrosophila model of human inherited triosephosphate isomerase deficiency glycolytic enzymopathy.
Heritable mutations, known as inborn errors of metabolism, cause numerous devastating human diseases, typically as a result of a deficiency in essential metabolic products or the accumulation of toxic intermediates. We have isolated a missense mutation in the Drosophila sugarkill (sgk) gene that causes phenotypes analogous to symptoms of triosephosphate isomerase (TPI) deficiency, a human famil...
متن کاملModulation of human triosephosphate isomerase gene transcription by serum.
We have monitored the level of mRNA encoding the glycolytic and gluconeogenic enzyme trisephosphate isomerase (TPI) during the growth arrest of cells by serum deprivation and the subsequent growth activation of cells by serum addition. This analysis has demonstrated that the steady state level of TPI mRNA changes 5-20-fold, depending upon the cell type, during the transversal of cells from a pr...
متن کاملIdentification of fibrillogenic regions in human triosephosphate isomerase.
Background. Amyloid secondary structure relies on the intermolecular assembly of polypeptide chains through main-chain interaction. According to this, all proteins have the potential to form amyloid structure, nevertheless, in nature only few proteins aggregate into toxic or functional amyloids. Structural characteristics differ greatly among amyloid proteins reported, so it has been difficult ...
متن کاملThe mechanism of the triosephosphate isomerase reaction.
The interconversion of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate catalyzed by the enzyme triosephosphate isomerase was first demonstrated by Meyerhof and Kiessling (1). Since then studies with the enzyme have disclosed little about the mechanism of this reaction. Such an interconversion may be envisioned as occurring by formation of an enediol as, based on chemical analogy (2)) ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44720-0