A Kinetic Study of the Phospholipase A2 (Crotalus adamanteus) Catalyzed Hydrolysis of l, 2-Dibutyryl-5n-glycero-3-phosphorylcholine

Biochemistry

Volumn 11, Issue 6, 1972, Pages 1030-1041

  Wells, Michael A ^a  

^a UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; BUTYRIC ACID DERIVATIVE; CALCIUM; LYSOPHOSPHATIDYLCHOLINE; PHOSPHATIDYLCHOLINE; PHOSPHOLIPASE; VENOM;

ANIMAL; ARTICLE; CATALYSIS; CHEMICAL MODEL; CHROMATOGRAPHY; ENZYME ACTIVATION; KINETICS; MATHEMATICS; PH; PROTEIN BINDING; SNAKE; SPECTROPHOTOMETRY; SYNTHESIS;

AMIDES; ANIMAL; BUTYRATES; CALCIUM; CATALYSIS; CHROMATOGRAPHY; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; KINETICS; LYSOPHOSPHATIDYLCHOLINES; MATHEMATICS; MODELS, CHEMICAL; PHOSPHATIDYLCHOLINES; PHOSPHOLIPASES; PROTEIN BINDING; SNAKES; SPECTROPHOTOMETRY; VENOMS;

EID: 0015505537     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00756a013     Document Type: Article

References (26)

1. Attwood, D. A., Saunders, L., Gammack, D. B., deHaas, G. H., and vanDeenen, L. L. M. (1965), Biochim. Biophys. Acta 102, 301.
2. Barton, P. G. (1968), J. Biol. Chem. 243, 3884.
3. Brockerhoff, H., and Yurkowski, M. (1965), Can. J. Biochem. 43, 1777.
4. Bird, P. R., deHaas, G. H., Heemskerk, C. H. T., and vanDeenen, L. L. M. (1965), Biochim. Biophys. Acta 98, 566.
5. Cleland, W. W. (1963a), Biochim. Biophys. Acta 67, 104.
6. Cleland, W. W. (1963b), Biochim. Biophys. Acta 67, 173.
7. Cleland, W. W. (1963c), Biochim. Biophys. Acta 67, 188.
8. Cleland, W. W. (1970), in The Enzymes, Vol. 2, Boyer, P. D., Ed., New York, N. Y., Academic Press, p 1.
9. Dawson, R. M. C. (1963a), Biochim. Biophys. Acta 70, 697.
10. Dawson, R. M. C. (1963b), Biochem. J. 88, 414.
11. de Haas, G. H., Bonsen, P. P. M., Pieterson, W. A., and van Deenen, L. L. M., (1971), Biochim. Biophys. Acta 239, 252.
12. Gaines, G. L., Jr. (1966), Insoluble Monolayers at LiquidGas Interfaces, New York, N. Y., Interscience, p 230.
13. Hanes, C. S., and Isherwood, F. A. (1949), Nature (London) 164, 1107.
14. Hauser, H., and Dawson, R. M. C. (1967), Eur. J. Biochem. 1, 61.
15. King, E. L., and Altman, C. (1956), J. Phys. Chem. 60, 1375.
16. Lineweaver, H., and Burk, D. (1938), J. Amer. Chem. Soc. 56, 658.
17. Phillips, G. S. C., and Williams, R. J. P. (1966), Inorganic Chemistry, Vol. II, Oxford, Oxford University Press, p 82.
18. Ray, Jr., W., and Roscelli, G. A. (1966), J. Biol. Chem. 241, 3499.
19. Roholt, O. A., and Schlamowitz, M. (1961), Arch. Biochem. Biophys. 94, 364.
20. Rojas, E., and Tobias, J. M. (1965), Biochim. Biophys. Acta 94, 394.
21. Saunders, D. R., and Wells, M. A. (1969), Biochim. Biophys. Acta 176, 828.
22. Tinker, D. O., and Pinteric, L. (1971), Biochemistry 10, 860.
23. vanDeenen, L. L. M., and de Haas, G. H. (1963), Biochim. Biophys. Acta 70, 538.
24. Wells, M. A. (1971a), Biochim. Biophys. Acta 248, 80.
25. Wells, M. A. (1971b), Biochemistry 10, 4074.
26. Wells, M. A., and Hanahan, D. J. (1969), Biochemistry 8, 414.