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お茶の水女子大學自然科學報告 >
45(1) >
| Title: | Purification and Characterization of an Acid Protease from Myxoamoebae of a True Slime Mold, Physarum polycephalum |
| Authors: | Minowa-Sonobe, Yukie
Shimada, Ynkiko
Murakami-Murofushi, Kimiko |
| NCID: | AN00033958 |
| Journal Title: | お茶の水女子大學自然科學報告 |
| Volume: | 45 |
| Issue: | 1 |
| Start Page: | 67 |
| End Page: | 78 |
| ISSN: | 00298190 |
| Issue Date: | 1994-07-15 |
| Publisher: | お茶の水女子大学 |
| Description: | 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 composition and specific activity of the purified enzyme were also very similar to those of the plasmodial protease. |
| Type: | Departmental Bulletin Paper |
| Appears in Collections: | 45(1)
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http://hdl.handle.net/10083/837
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