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Biomedical subjects

H Sandermann

Publications and source records attributed to H Sandermann.

101 records · Page 6Linked to original sources
PubMed1971

C 55 -isoprenoid alcohol phosphokinase: an extremely hydrophobic protein from the bacterial membrane.

C(55)-isoprenoid alcohol phosphokinase, a butanol-soluble enzyme from the membrane of Staphylococcus aureus, has been purified to homogeneity by the inclusion of organic solvents in all of the techniques used. By polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the enzyme is a single polypeptide chain of molecular weight 17,000. The amino-acid analysis reveals an unusually high content of nonpolar amino acids (58%), the largest amount so far reported in any protein. When equilibrated in butanol-water, enzyme apoprotein is found in the butanol layer. The influence of sodium chloride indicates that the lipid requirement of the enzyme is nonelectrostatic in nature.

Alcohols↗
PubMed1970

Transfer of apiose from UDP-apiose to 7-O-(beta-D-glucosyl)-apigenin and 7-O-(beta-D-glucosyl)-chrysoeriol with an enzyme preparation from parsley.

An enzyme preparation from parsley (Petroselinum hortense Hoffm.) catalyses the formation of apiin (7-O-[beta-D-apio-furanosyl(1-->2)beta-D-glycosyl]-5,7,4'-trihydroxyflavone) from 7-O-(beta-D-glycosyl)-apigenin and UDP-apiose and of the corresponding chrysoeriol-7-apiosyl-glucoside from 7-O(beta-D-glucosyl)-chrysoeriol and UDP-apiose. Neither free apiose nor cyclic apiose-1,2-phosphate can function as a substrate for the transfer reaction.

Journal Article↗