THE EFFECT OF GAMMA RADIATION ON THE AMINO ACID CONTENT AND THE ENZYMATIC ACTIVITY OF ATP-CREATINE PHOSPHOTRANSFERASE
In the intact protein in solution, histidine is most radiosensitive, but in the corresponding amino acid hydrolyzate in solution, methionine is most labile. Phenylalanine and arginine are also faster destroyed if the protein is hydrolyzed befoie radiation exposure. Since rank in terms of radiation lability varies with individual proteins, stereochemical orientation (amino acid sequence) must be suspected as a determinant. Reconstitution of some amino acids by interconversion during radiation exposure enhances apparent stability of glutamic and aspartic acids, for instance, and their G values with reference to the protein have a destructive and a constructive component. Sulihydryl (--SH) groups disappear at a faster rate than other amino acid side chains, and decline in enzymic activity is even more rapid than destruction of --SH groups. No decision, however, was reached as to whether destruction of --SH side chains or disruption of protein configuration causes the loss of enzyme activity in the early stages of gamma irradiation. (auth)
- Research Organization:
- Howard Univ., Washington, D.C.
- Sponsoring Organization:
- USDOE
- NSA Number:
- NSA-16-031645
- OSTI ID:
- 4777485
- Journal Information:
- Archives of Biochemistry and Biophysics (U.S.), Journal Name: Archives of Biochemistry and Biophysics (U.S.) Vol. Vol: 98; ISSN ABBIA
- Country of Publication:
- Country unknown/Code not available
- Language:
- English
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