Partial purification and properties of cathepsin G-like proteinase of mouse myeloid leukemia M1 cells.
A proteinase extracted with 1M NaCl from particulate fraction of the postnuclear fraction of mouse myeloid leukemia M1 cells was partially purified by Bio-Gel HTP treatment and Sephadex G-75 gel filtration. The apparent molecular mass of the proteinase was 26,000 Da and the isoelectric point was about pH 10. The enzyme activity was inhibited by phenylmethanesulfonylfluoride, chymostatin, and soy-bean trypsin inhibitor. It hydrolysed specifically Suc-Ala2-Pro-Phe-4-methylcoumaryl-4-amide (MCA). NaCl and KCl enhanced several times the activity for Suc-Ala2-Pro-Phe-MCA, but not that for fluorescein-labeled albumin and fibrinogen. These enzymic properties of the major proteinase are similar to those of chymotrypsin and cathepsin G. The role of a cathepsin G-like proteinase in relation to M1 cell differentiation is discussed.
Oshima
G
G
School of Pharmaceutical Sciences, Kitasato University, Tokyo.
Yamada
M
M
Sugimura
T
T
D000595:Amino Acid Sequence; D000818:Animals; D056649:Cathepsin G; D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D015470:Leukemia, Myeloid, Acute / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D012492:Salts / Q000494:pharmacology; D012697:Serine Endopeptidases; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured / Q000201:enzymology
D012492:Salts; D002403:Cathepsins; D012697:Serine Endopeptidases; D056649:Cathepsin G; C534096:Ctsg protein, mouse