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Current IssueEditorial BoardOnline First ArticlesArchive

volume 39 issue 2 (july to december 2005) : 123 - 126

KINETICS OF ALKALINE PHOSPHATASE ISOLATED FROM RAT LIVER, KIDNEY AND CERTAIN BRAIN REGIONS

N
N.H. Mohan1
S
S.K. Maurya
A
A.K Gangwar
R
R.S. Srivastava2
1Department of Veterinary Physiology, College of Veterinary Science and A.H., NDUAT, Kumarganj, Faizabad (UP) - 224 229, India

  • Submitted|

  • First Online |

  • doi

Cite article:- Mohan1 N.H., Maurya S.K., Gangwar A.K, Srivastava2 R.S. (2025). KINETICS OF ALKALINE PHOSPHATASE ISOLATED FROM RAT LIVER, KIDNEY AND CERTAIN BRAIN REGIONS. Indian Journal of Animal Research. 39(2): 123 - 126. doi: .

ABSTRACT

In the present study, the kinetics of alkaline phosphatase (ALP) isoforms partially purified
from rat liver, kidney, hypothalamus and cerebro-cortical region of brain is reported. The MichaelisMenten
constant (Km,micromoles) of the enzyme for the substrate p-nitrophenyl phosphate
were 2.67,2.50 2.85 and 3.33 for the enzymes-obtainecJ-from liver, kidney, hypothalamus and
cortical region respectively. The corresponding V..... values (nanomoles/milligram protein/minute)
were 1.03, 1.43, 1.33 and 2.22 respectively. The fraction of catalytic sites filled in the enzyme
by the substrate was also calculated. For any substrate concentration, the fraction of catalytic
sites filled was highest for renal ALP and lowest for cortical one. The variation in the properties
of these tissue specific or unspecific enzymes may be due to differential expression of ALP
genes or post-translational modifications. Since there was no significant difference between
these values it was concluded that the kinetics of ALP for p-nitrophenyl phosphate substrate
alone is not sufficient to distinguish these clinically important isoforms

KEYWORDS

    REFERENCES

    1. Berg. J.M. et al. (2002). Biochemistry. W.H. Freeman and Company, New York, 200-222.
    2. Goldstein, D.L. et al. (1980). Proc. Natl. Acad. Sci. USA, 77: 2857-2860.
    3. Hodson. AW. et al. (1963). Clin. Chern. Acta., 9: 255-261.
    4. Hoffman. W.E.et al. (1983). Enzymes, 30: 269-275.
    5. Lowry, O.H. et al. (1951). 1. Bioi. Chem., 193: 265-275.
    6. Noguchi. T. and Yamashita, Y. (1987). Biochem. Biophy. Res. Commn., 143: 15-20.
    7. Raphael, 5.5. (1976). Lynch's Medical Laboratory Technology. 3rd ed, W.B. Saunders, Philidelphia, 271-277.
    8. Saini. P.K a~d Saini, S.K. (1978a). Am. J. Vet. Res., 39: 1506-1509.
    9. Saini. P.K et al. (1978b). Am. J. Vet. Res., 39: 1514-1518.
    10. Stigbrand. T. et al. (1982). In: Isozymes:Current Topics in Biological and Medical Research. (Rallazzi, M.C. et al.. eds). 6: 93-117.
    11. Wellman. M.L. et al. (1982). Am. J. Vet. Res.. 43: 1204-1207.
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    Indian Journal of Animal Research
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      volume 39 issue 2 (july to december 2005) : 123 - 126

      KINETICS OF ALKALINE PHOSPHATASE ISOLATED FROM RAT LIVER, KIDNEY AND CERTAIN BRAIN REGIONS

      N
      N.H. Mohan1
      S
      S.K. Maurya
      A
      A.K Gangwar
      R
      R.S. Srivastava2
      1Department of Veterinary Physiology, College of Veterinary Science and A.H., NDUAT, Kumarganj, Faizabad (UP) - 224 229, India

      • Submitted|

      • First Online |

      • doi

      Cite article:- Mohan1 N.H., Maurya S.K., Gangwar A.K, Srivastava2 R.S. (2025). KINETICS OF ALKALINE PHOSPHATASE ISOLATED FROM RAT LIVER, KIDNEY AND CERTAIN BRAIN REGIONS. Indian Journal of Animal Research. 39(2): 123 - 126. doi: .

      ABSTRACT

      In the present study, the kinetics of alkaline phosphatase (ALP) isoforms partially purified
      from rat liver, kidney, hypothalamus and cerebro-cortical region of brain is reported. The MichaelisMenten
      constant (Km,micromoles) of the enzyme for the substrate p-nitrophenyl phosphate
      were 2.67,2.50 2.85 and 3.33 for the enzymes-obtainecJ-from liver, kidney, hypothalamus and
      cortical region respectively. The corresponding V..... values (nanomoles/milligram protein/minute)
      were 1.03, 1.43, 1.33 and 2.22 respectively. The fraction of catalytic sites filled in the enzyme
      by the substrate was also calculated. For any substrate concentration, the fraction of catalytic
      sites filled was highest for renal ALP and lowest for cortical one. The variation in the properties
      of these tissue specific or unspecific enzymes may be due to differential expression of ALP
      genes or post-translational modifications. Since there was no significant difference between
      these values it was concluded that the kinetics of ALP for p-nitrophenyl phosphate substrate
      alone is not sufficient to distinguish these clinically important isoforms

      KEYWORDS

        REFERENCES

        1. Berg. J.M. et al. (2002). Biochemistry. W.H. Freeman and Company, New York, 200-222.
        2. Goldstein, D.L. et al. (1980). Proc. Natl. Acad. Sci. USA, 77: 2857-2860.
        3. Hodson. AW. et al. (1963). Clin. Chern. Acta., 9: 255-261.
        4. Hoffman. W.E.et al. (1983). Enzymes, 30: 269-275.
        5. Lowry, O.H. et al. (1951). 1. Bioi. Chem., 193: 265-275.
        6. Noguchi. T. and Yamashita, Y. (1987). Biochem. Biophy. Res. Commn., 143: 15-20.
        7. Raphael, 5.5. (1976). Lynch's Medical Laboratory Technology. 3rd ed, W.B. Saunders, Philidelphia, 271-277.
        8. Saini. P.K a~d Saini, S.K. (1978a). Am. J. Vet. Res., 39: 1506-1509.
        9. Saini. P.K et al. (1978b). Am. J. Vet. Res., 39: 1514-1518.
        10. Stigbrand. T. et al. (1982). In: Isozymes:Current Topics in Biological and Medical Research. (Rallazzi, M.C. et al.. eds). 6: 93-117.
        11. Wellman. M.L. et al. (1982). Am. J. Vet. Res.. 43: 1204-1207.
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          Indian Journal of Animal Research

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