Carboxypeptidase Y and invertase from baker’s yeast, Saccharomyces cerevisiae, have two classes of Nlinked high mannose oligosaccharides which may be distinguished on the basis of their susceptibility to hydrolysis by endo-8-N-acetylglucosaminidase H (Endo H). Thus, three of the four oligosaccharides on carboxypeptidase Y and seven of nine of those on invertase are readily released by Endo H wh...

Utilization of sucrose as a source of carbon and energy in yeast (Saccharomyces) is controlled by the classical SUC genes, which confer the ability to produce the sucrose-degrading enzyme invertase (Mortimer and Hawthorne 1969). Mutants of S. cerevisiae strain S288C (SUC2+) unable to grow anaerobically on sucrose, but still able to use glucose, were isolated. Two major complementation groups we...

The initial step of disaccharide dissimilation by Actinomyces viscosus serotype 2 strain M-100 was studied. Sucrase activity was found in the 3,000 X g particulate fraction and the 37,000 X g soluble fraction of the cells, whereas lactase activity was found almost exclusively in the 37,000 X g soluble fraction. Neither sucrase nor lactase activity was appreciable in the culture liquor. Sucrose ...

When the rate of hydrolysis of sucrose, by invertase from honey, is plotted against time, the graph obtained was found, by Nelson and Cohn (I), to indicate an acceleration at the beginning of the reaction. The effect is represented by the first part of Curve C .in Fig. 1. This increase in the rate of hydrolysis is rather unusual since invertase action, when the invertase is obtained from bottom...

The assembly of functional proteins from fragments in vivo has been recently described for several proteins, including the secreted maltose binding protein in Escherichia coli. Here we demonstrate for the first time that split gene products can function within the eukaryotic secretory system. Saccharomyces cerevisiae strains able to use sucrose produce the enzyme invertase, which is targeted by...

Three soluble isoforms of invertase (8-fructofuranosidase; EC 3.2.1.26) were purified from 7-d-old primary leaves of barley (Hordeum vurgare 1.). lnvertase I, a monomeric protein of 64 kD, was purified to apparent homogeneity as shown by sodium dodecylsulfate-polyacrylamide gel electrophoresis. lnvertases IIA and IIB, multimeric proteins with molecular masses of 116 and 155 kD, were purified 78...