Studies on Enzymatically Active Subfragments of Myosin Adenosine Triphosphatase:II. Preparation by Nagarse Digestion and Comparison with Subfragments Prepared by Using Different Proteolytic Enzymes
-
- YAZAWA Yoichi
- Department of Chemistry, Faculty of Science, Hokkaido University
-
- YAGI Koichi
- Department of Chemistry, Faculty of Science, Hokkaido University
この論文をさがす
説明
An enzymatically active subfragment of myosin was isolated by Nagarse-digestion of myosin. It was shown to be homogeneous by the determinations of ultracentrifuge, gel filtration of Sephadex G-200 and polyacrylamide-gel electrophoresis. Physical parameters of the subfragment were similar to those of other subfragments prepared by tryptic, chymotryptic, or papain digestion. The subfragment binds strongly to F-actin at the molar ratio of 1, but the activity of actin-activated Mg-ATPase was very low and the acceleration of actin polymerization was hardly observed.<BR>The number of moles of N-terminal amino acids of the subfragment was about 2.62 moles per mole, which suggests an intramolecular peptide bond cleavage. It was also indicated by intrinsic viscosity and gel-filtration chromatography obtained in 5 M guanidine-HCl. In 5 M guanidine-HCl, the subfragment separated into two components and the molecular weight of one component of 32.2 per cent in weight was 4.3×104 and that of another component of 64.8 per cent in weight was about 1.8×104.<BR>The properties were compared with those of the subfragments prepared by using chymotrypsin, trypsin, and trypsin-Nagarse as proteolytic enzymes. Similar results were obtained with the subfragment prepared by tryptic digestion of heavymeromyosin. The extent of proteolysis was less in the one digested by chymotrypsin and more in trypsin-Nagarse than the one digested with Nagarse or trypsin.
収録刊行物
-
- The Journal of Biochemistry
-
The Journal of Biochemistry 73 (3), 567-580, 1973
The Japanese Biochemical Society
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1573668927917474048
-
- NII論文ID
- 130003538989
-
- ISSN
- 0021924X
-
- 本文言語コード
- en
-
- データソース種別
-
- CiNii Articles