PubMed Health⌕ Search

Biomedical subjects

H Murofushi

Publications and source records attributed to H Murofushi.

79 records · Page 5Linked to original sources

Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization.

A calcium-activated neutral protease was purified 2,700-fold over the crude extract from chicken skeletal muscle. The purified protease migrated as a single band on polyacrylamide gel electrophoresis with or without SDS. Its molecular weight was 80,000 and pH optimum for activity was 7.7. The activity required strictly the presence of calcium (optimum concentration: 1.8 mM) or strontium (optimum concentration: 10 mM) ions. The protease was inhibited by leupeptin, which is known to be a strong inhibitor of papain, cathepsin B, trypsin, and plasmin.

Amino Acids↗

Electrophoretic separation of tubulin alpha and beta subunits after S-sulfonation.

The modification of tubulin cystine and cystine residues to S-sulfocysteines caused a distinct separation of the alpha and beta subunits in a continuous sodium dodecyl sulfate polyacrylamide gel system. The well-separated subunit bands permitted investigation of the phosphorylation of alpha and beta tubulin subunits. The incubation of tubulin fraction with [gamma-32P]ATP demonstrated that both subunits were phosphorylated in vitro. The incorporation of 32-PO4 into sea urchin eggs, however, failed to cause phosphorylation of tubulin in vivo.

Adenosine Triphosphate↗