Two molecular forms of adenosine deaminase have been isolated from bovine livers. These two forms were found to be interconvertible. Adenosine deaminase extracted from human tissues exhibited similar properties as well. Previous studies have shown the presence of a conversion factor which formed an aggregate with the small form (the C-form) of the enzymes, and the resulting enzyme complex was identified to be the large form (the A-form) of adenosine deaminase. Studies have been made with rat tissues. The C-form of the adenosine deaminase is widely distributed in the various tissues, while the large form of the enzyme is absent in those tissues examined.The outline of this study is summarized below: (1) The isolation of the conversion factor from human liver.(2) The isolation of the adenosine deaminase from the various tissues.(3) The coversion of human adenosine deaminase C-form to the A-form.(4) Quantization of the conversion of the C-form to the A-form.(5) Testing the effect of conversion on nonhuman enzymes.(6) The optimum temperature and time to yield greatest amount of conversion.The results from this study would verify any differences that might exist between the small forms of the enzyme present in different species.
| Identifer | oai:union.ndltd.org:BSU/oai:cardinalscholar.bsu.edu:handle/182409 |
| Date | January 1981 |
| Creators | Puttaswamy, Shashi |
| Contributors | Ma, Pang-Fai |
| Source Sets | Ball State University |
| Detected Language | English |
| Format | viii, 48 leaves : ill. ; 28 cm. |
| Source | Virtual Press |
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