Phosphopyruvate Carboxylase from Bakers' Yeast
نویسندگان
چکیده
منابع مشابه
DNA polymerases from bakers' yeast.
Two DNA polymerases are present in extracts of commercial bakers' yeast and wild type Saccharomyces cerevisiae grown aerobically to late log phase. Yeast DNA polymerase I and yeast DNA polymerase II can be separated by DEAE-cellulose, hydroxylapatite, and denatured DNA-cellulose chromatography from the postmitochondrial supernatants of yeast lysates. The yeast polymerases are both of high molec...
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In the course of studies of formaldehyde metabolism in yeast (I), an enzyme was found that catalyzed the oxidation of formaldehyde in the presence of glutathione and diphosphopyridine nucleotide. A similar enzyme was discovered independently by Strittmatter and Ball in liver (2). This paper describes the partial purification and some of the properties of yeast formaldehyde dehydrogenase. Some e...
متن کاملCytoplasmic Methionyl - tRNA Synthetase from Bakers ’ Yeast
Methionyl-tRNA synthetase has been purified from a yeast strain carrying the MESl structural gene on a high copy number plasmid (pFL1). The purified enzyme is a monomer of M, = 85,000 in contrast to its counterpart from Escherichia coli which is a dimer made up of identical subunits (M, = 76,000; Dardel, F., Fayat, G., and Blanquet, S . (1984) J. Bucteriol. 160,1115-1122). The yeast enzyme was ...
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Purified cytochrome c oxidase from bakers’ yeast can be resolved into six polypeptide bands by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The apparent molecular weights of these components are I, 42,000; II, 34,500; III, 23,000; IV, 14,000; V, 12,500; and VI, 9,500. (Although Component V actually consists of two distinct polypeptide species, it will be regarde...
متن کاملCytochrome c Oxidase from Bakers’ Yeast
Cytochrome aa3 was purified 35to 40-fold from submitochondrial particles of commercial bakers’ yeast. The purification procedure involved solubilization of the enzyme with cholate, fractionation with ammonium sulfate, and chromatography on DEAE-cellulose in the presence of Triton x-100. The purified, active enzyme contained approximately 10 nmoles of heme a per mg of protein and was free of oth...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1963
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)67920-7