The separation of lactate dehydrogenase X from other lactate dehydrogenase isozymes of mouse testes by affinity chromatography
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چکیده
منابع مشابه
Isolation of human lactate dehydrogenase isoenzyme X by affinity chromatography.
Human isoenzyme LDH-X (lactate dehydrogenase isoenzyme X) was isolated from seminal fluid of frozen semen samples by affinity chromatography by using oxamate-Sepharose and AMP-Sepharose. In the presence of 1.6 mM-NAD+, isoenzyme LDH-X does not bind to AMP-Sepharose, whereas the other lactate dehydrogenase isoenzymes do. This is the crucial point in the isolation of isoenzyme LDH-X from the othe...
متن کاملSeparation of rat lactate dehydrogenase isoenzyme C4 from other isoenzymes by affinity and ion-exchange chromatography.
Lactate dehydrogenase C, an isoenzyme composed of C polypeptide subunits and found only in mature testes and spermatozoa, differs kinetically, chemically and immunologically from the five common isoenzymes of lactate dehydrogenase, each of which is a tetramer of A and/or B subunits. In the rat lactate dehydrogenase C exists in two molecular forms, isoenzymes C4 and A1C3. In addition to these tw...
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NH,CI. None of the adaptations could be attributed to the high-protein diet per se since they were not evident in those rats fed a high-protein diet and given NaHC03 solution to drink. Of particular interest is the increased rate of gluconeogenesis found in kidney slicesfrom rats fed ona high-protein diet. Krebs et al. (1963) have observed an increased rate of renal gluconeogenesis in rats fed ...
متن کاملAffinity chromatography of lactate dehydrogenase on immobilized nucleotides.
The interaction of two isoenzymes of lactate dehydrogenase from pig heart muscle (H(4)) and rabbit skeletal muscle (M(4)), with immobilized nucleotides was examined: the effects of pH and temperature on the binding of lactate dehydrogenase were studied with immobilized NAD(+) matrices. The influence of substrate, product and sulphite on the binding of heart muscle lactate dehydrogenase to immob...
متن کاملAmino Acid Composition and Properties of Crystalline Lactate Dehydrogenase X from Mouse Testes*
Lactate dehydrogenase (LDH) X has been isolated in crystalline form from mouse testes. Homogeneity of the protein preparation was established by disc gel electrophoresis, analytical ultracentrifugation, and immunochemical analyses. LDH-X is clearly distinct in amino acid composition from LDH-1 and LDH-5 with respect to numbers of residues of leucine, glycine, threonine, and methionine. When 6 t...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1973
ISSN: 0014-5793
DOI: 10.1016/0014-5793(73)80568-x