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H Matthaei

Publications and source records attributed to H Matthaei.

At least 37 records · Page 2Linked to original sources
PubMed1971

The role of cholesteryl 14-methylhexadecanoate in peptide elongation reactions.

1. Peptide-elongation factors were purified from rat liver and human tonsils and the contents of cholesteryl 14-methylhexadecanoate were determined in fractions obtained during enzyme purification. The relative contents of this compound in purified enzyme preparations was several times higher than that in the crude starting material. Elongation factors from human tonsils contained a significantly larger quantity of the cholesteryl ester than enzyme from rat liver. 2. Transfer enzymes extracted with various organic solvents showed variable decreased activities in both binding and peptidization assay. The decrease of enzymic activity was proportional to the amount of cholesteryl 14-methylhexadecanoate extracted from a given enzymic preparation. In systems containing both extracted elongation factors the polyphenylalanine synthesis was limited by the residual activity of the less active transfer factor. 3. The original enzymic activity of extracted transferases was fully recovered by the addition of pure cholesteryl 14-methylhexadecanoate in quantities corresponding to those extracted. 4. Increase of the relative contents of this cholesteryl ester during enzyme purification, decrease of the enzymic activity after the extraction and its recovery by the addition of this compound indicates that the presence of this ester in elongation factors is essential for the normal function of these enzymes.

Amino Acids↗
PubMed1970

Solubilized DNA-dependent RNA polymerase from human placenta: A Mn(2+)-dependent enzyme.

The 100-fold purified RNA polymerase activity from human placenta is completely dependent upon added DNA. The enzyme is most active at 3 mM Mn(2+) in the presence of 100 mM (NH(4))(2)SO(4). Denatured DNA is a better template than native DNA. alpha-Amanitin completely inhibits the incorporation of 3H-UMP, while rifampicin has no influence upon the enzymatic activity.

Journal Article↗