Biochemical Study on Histidine Synthesis in Cattle Liver
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Accession number;05A1044279
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| Title;Biochemical Study on Histidine Synthesis in Cattle Liver |
| Author;
TAKAHASHI TOSHIHIRO
(Miyazaki Univ., Faculty of Agriculture, JPN)
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Journal Title;Shokuniku ni kansuru Josei Kenkyu Chosa Seika Hokokusho
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Journal Code:X0296A
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ISSN:
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VOL.23;NO.;PAGE.143-147(2005)
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| Figure&Table&Reference;FIG.2, TBL.3, REF.9 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;The present experiments were conducted to extract and purify the histidinol dehydrogenase (HisD) enzyme from cattle liver, in order to clarify the difference of HisD activity and histidine biosynthesis capacity between the animals. In experiment 1, four salt precipitated fractions (30%, 30-45%, 45-60%, 60-75% ammonium sulfate precipitation) and cytosol fraction were prepared from cattle liver homogenate using centrifugation method. Each fraction was used as crude enzyme solutions for the measurement of HisD specific activities. The histidine producing activity from histidinol by the enzymes of liver cytosol was observed in 45-75% salt precipitated fractions. This means that the enzyme which has HisD activity in the animal tissues is similar to HisD in plant cell. In experiment 2, five salt precipitated fractions (45-50%, 50-55%, 55-60%, 60-65%, 60-65% and 65-70% ammonium sulfate precipitattion) were prepared from cattle liver. The histidine producing activity of 60-65% salt precipitated fractions is about 2.5 times higher than their cytosol fraction, and that contains characteristic 45 to 55 KD protein. In experiment 3, the time-dependent reduction of HisD activity was investigated, and the activity disappeared when enzyme solutions were stored at 4 .DEG.C. for 7 days. Although the activity of 60-65% salt precipitated fraction was notedly high until 3 days after. (author abst.) |
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