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- W223374129 abstract "ABSTRACT In the yeast cell wall a number of hydrolytic enzymes are located. Some of them were found to be glycoproteins. Our interest was centered on acid phosphatase, an inducible enzyme of the yeast Saccharomyces cerevisiae. The enzyme was purified to a high degree, and it was found that it contained about 50% of covalently bound carbohydrates (95% mannose with traces of glucose and 5% N-ace-tylglucosamine). The enzyme preparation contained a whole range of molecules, having the same protein part and differing in the carbohydrate content. It was shown that the reason of this difference was not the various number of carbohydrate chains per molecule, but rather different lenghts of these chains. The molecular weight of the enzyme was found to be 286 000 and it consisted of two identical subunits. Amino acid analysis showed that the enzyme contained the greatest percentage of aspartic and glutamic acids and a small quantity of basic amino acids. This indicated an acidic character of the molecules, what was further confirmed by isoelectric focusing; the major enzyme fraction was isoelectric at pH 4.25. The composition and structure of the isolated glycopeptides from acid phosphatase were also studied. The obtained results indicated that the structure of sugar chains was closely related to the yeast mannan structure, and that the carbohydrate parts of acid phosphatase and invertase were very similar." @default.
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- W223374129 date "1980-01-01" @default.
- W223374129 modified "2023-10-16" @default.
- W223374129 title "ACID PHOSPHATASE, A GLYCOPROTEIN OF THE YEAST CELL WALL" @default.
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- W223374129 doi "https://doi.org/10.1016/b978-0-08-024417-4.50013-5" @default.
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