Multiple forms of human adenosine deaminase. II. Isolation and properties of a conversion factor from human lung

作者: Hiromu Nishihara , Satsuki Ishikawa , Kiyoko Shinkai , Hitoshi Akedo

DOI: 10.1016/0005-2744(73)90172-1

关键词:

摘要: Abstract 1. A conversion factor, which can convert the small form ( E S ; 47 000 mol. wt) of human adenosine deaminase (EC 3.5.4.4) to large L 230 wt), was purified about 600-fold from normal lung by (NH4)2SO4 fractionation, Sephadex and DEAE-cellulose chromatography, preparative acrylamide electrophoresis. 2. The preparation, heat labile free activity, exhibited upon disc electrophoresis a single protein band associated with converting activity also showed maximum absorption at 280 nm. Its molecular weight found be 139 when judged gel filtration G-200. 3. factor did not require sulfhydryl compounds nor bivalent metal ions for exerting its activity. 4. Results quantitative analysis rate formation known amounts , immunochemical characterizations two forms enzyme in relation using antiserum against polyacrylamide presence sodium dodecyl sulfate strongly suggest that is complex factor. 5. No detectable demonstrated an extract cancer tissue.

参考文章(13)
Hitoshi Akedo, Hiromu Nishihara, Kiyoko Shinkai, Keiko Komatsu, Satsuki Ishikawa, Multiple forms of human adenosine deaminase: I. Purification and characterization of two molecular species Biochimica et Biophysica Acta. ,vol. 276, pp. 257- 271 ,(1972) , 10.1016/0005-2744(72)90028-9
Robert G. Martin, Bruce N. Ames, A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein Mixtures Journal of Biological Chemistry. ,vol. 236, pp. 1372- 1379 ,(1961) , 10.1016/S0021-9258(18)64180-8
E.M. Reimann, C.O. Brostrom, J.D. Corbin, C.A. King, E.G. Krebs, Separation of regulatory and catalytic subunits of the cyclic 3′, 5′-adenosine monophosphate-dependent protein kinase(s) of rabbit skeletal muscle Biochemical and Biophysical Research Communications. ,vol. 42, pp. 187- 194 ,(1971) , 10.1016/0006-291X(71)90086-6
Hitoshi Akedo, Hiromu Nishihara, Kiyoko Shinkai, Keiko Komatsu, Adenosine deaminases of two different molecular sizes in human tissues Biochimica et Biophysica Acta (BBA) - Enzymology. ,vol. 212, pp. 189- 191 ,(1970) , 10.1016/0005-2744(70)90196-8
Gordon N. Gill, Leonard D. Garren, A cyclic-3′,5′-adenosine monophosphate dependent protein kinase from the adrenal cortex: Comparison with a cyclic AMP binding protein Biochemical and Biophysical Research Communications. ,vol. 39, pp. 335- 343 ,(1970) , 10.1016/0006-291X(70)90581-4
A. Chrambach, R.A. Reisfeld, M. Wyckoff, J. Zaccari, A procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresis Analytical Biochemistry. ,vol. 20, pp. 150- 154 ,(1967) , 10.1016/0003-2697(67)90272-2
R. A. REISFELD, U. J. LEWIS, D. E. WILLIAMS, Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide Gels Nature. ,vol. 195, pp. 281- 283 ,(1962) , 10.1038/195281A0
Akira Kumon, Hirohei Yamamura, Yasutomi Nishizuka, Mode of action of adenosine 3',5'-cyclic phosphate on protein kinase from rat liver. Biochemical and Biophysical Research Communications. ,vol. 41, pp. 1290- 1297 ,(1970) , 10.1016/0006-291X(70)90228-7
Baruch J. Davis, DISC ELECTROPHORESIS - II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS* Annals of the New York Academy of Sciences. ,vol. 121, pp. 404- 427 ,(2006) , 10.1111/J.1749-6632.1964.TB14213.X