Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1962 Dec;85(3):576–580. doi: 10.1042/bj0850576

Specificity and properties of wheat-germ esterase

L A Mounter 1, Mary-Elizabeth Mounter 1
PMCID: PMC1243784  PMID: 13936331

Full text

PDF
576

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ALDRIDGE W. N. Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination. Biochem J. 1953 Jan;53(1):110–117. doi: 10.1042/bj0530110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ALDRIDGE W. N. Serum esterases. II. An enzyme hydrolysing diethyl p-nitrophenyl phosphate (E600) and its identity with the A-esterase of mammalian sera. Biochem J. 1953 Jan;53(1):117–124. doi: 10.1042/bj0530117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. ALDRIDGE W. N. Some esterases of the rat. Biochem J. 1954 Aug;57(4):692–702. doi: 10.1042/bj0570692. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DESNUELLE P. Hydrolyse enzymatique des triglycérides. Bull Soc Chim Biol (Paris) 1951;33(8):909–923. [PubMed] [Google Scholar]
  5. DESNUELLE P. Pancreatic lipase. Adv Enzymol Relat Subj Biochem. 1961;23:129–161. doi: 10.1002/9780470122686.ch4. [DOI] [PubMed] [Google Scholar]
  6. EADIE G. S. On the evaluation of the constants Vm and Km in enzyme reactions. Science. 1952 Dec 19;116(3025):688–688. doi: 10.1126/science.116.3025.688. [DOI] [PubMed] [Google Scholar]
  7. GAWRON O., GRELECKI C. J., DUGGAN M. The effect of substituents on the hydrolysis of phenyl acetate by wheat germ lipase. Arch Biochem Biophys. 1953 Jun;44(2):455–467. doi: 10.1016/0003-9861(53)90063-0. [DOI] [PubMed] [Google Scholar]
  8. MOUNTER L. A., DIEN L. T. Dialkylfluorophosphatase of kidney. V. The hydrolysis of organophosphorus compounds. J Biol Chem. 1956 Apr;219(2):685–690. [PubMed] [Google Scholar]
  9. MOUNTER L. A., TUCK K. D., ALEXANDER H. C., 3rd, DIEN L. T. The reactivity of esterases and proteases in the presence of organophosphorus compounds. J Biol Chem. 1957 Jun;226(2):873–879. [PubMed] [Google Scholar]
  10. MOUNTER L. A. The specificity of cobra-venom cholinesterase. Biochem J. 1951 Nov;50(1):122–128. [PMC free article] [PubMed] [Google Scholar]
  11. MOUNTER L. A., WHITTAKER V. P. The esterases of horse blood; the specificity of horse erythrocyte cholinesterase. Biochem J. 1950 Nov-Dec;47(5):525–530. doi: 10.1042/bj0470525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Murray D. R. Molecular constitution and accessibility to enzymes: The effect of various substances on the velocity of hydrolysis by pancreatic lipase. Biochem J. 1929;23(2):292–308. doi: 10.1042/bj0230292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. SARDA L., DESNUELLE P. Action de la lipase pancréatique sur les esters en émulsion. Biochim Biophys Acta. 1958 Dec;30(3):513–521. doi: 10.1016/0006-3002(58)90097-0. [DOI] [PubMed] [Google Scholar]
  14. STURGE L. M., WHITTAKER V. P. The esterases of horse blood; the specificity of horse plasma cholinesterase and ali-esterase. Biochem J. 1950 Nov-Dec;47(5):518–525. doi: 10.1042/bj0470518. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. WHITTAKER V. P. Specificity, mode of action and distribution of cholinesterases. Physiol Rev. 1951 Jul;31(3):312–343. doi: 10.1152/physrev.1951.31.3.312. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES