@article{oai:teapot.lib.ocha.ac.jp:00034714,
 author = {Minowa-Sonobe, Yukie and Shimada, Ynkiko and Murakami-Murofushi, Kimiko},
 issue = {1},
 journal = {お茶の水女子大學自然科學報告},
 month = {Jul},
 note = {application/pdf, 紀要論文, In order to compare the characteristics of acid protease (s) in diploid and haploid cells of a true slime mold, Physarum polycephalum, an acid protease was purified from the haploid myxoamoebae of Physarum by a combination of detergent extraction, acid precipitation, and ion-exchange column chromatographies. The purified enzyme having a molecular weight of 68,000 was composed of two polypeptide chains, 31-kDa heavy chain and 23-kDa light chain. These polypeptides were cross-linked by disulfide bond (s), and the heavy chain contained carbohydrate moiety composed of mannose, glucosamine, fucose and glucose. Optimum pH of the enzyme reaction was 1.7 toward hemoglobin as a substrate. A typical aspartic protease inhibitor, diazoacetyl-D, L-norleucine methyl ester (DAN), inhibited the enzyme activity in the presence of cupric ions, but the enzyme was not sensitive to the other aspartic protease inhibitors, 1, 2-epoxy-3-(p-nitrophenoxy) propane (EPNP) and pepstatin A. These results indicate that the characteristics of the amoeboid protease is very similar to those of the plasmodial enzyme. In addition, amino acid compositio\
n and specific activity of the purified enzyme were also very similar to those of the plasmodial protease.},
 pages = {67--78},
 title = {Purification and Characterization of an Acid Protease from Myxoamoebae of a True Slime Mold, Physarum polycephalum},
 volume = {45},
 year = {1994}
}