PHOSPHATE AND MANNOSE TRANSFER FROM GUANOSINE DIPHOSPHATE MANNOSE TO YEAST MANNAN ACCEPTORS

被引:19
作者
BRETTHAUER, RK
KOZAK, LP
IRWIN, WE
机构
[1] Department of Chemistry, Program in Biochemistry and Biophysics, University of Notre Dame, Notre Dame
关键词
D O I
10.1016/0006-291X(69)90965-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A particulate enzyme isolated from Hansenula holstii catalyzes the transfer of 14C-mannose from guanosine diphosphate 14C-mannose and of 32P-phosphate from β-32P-guanosine diphosphate mannose to endogenous acceptor molecules. The 32P-product is solubilized with Tris buffer, excluded from Sephadex G-50 and precipitated with Fehling's reagent.32P-Mannose 6-phosphate is recovered from acid hydrolyzates. Mild acid hydrolysis liberates newly incorporated mannose residues and allows the 32P-phosphate to be released as inorganic phosphate by phoshomonoesterase. The synthesis of a 1, 6′-phosphodiester linkage between 2 mannose residues is proposed. © 1969.
引用
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页码:820 / +
页数:1
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