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. 1954 Aug;57(4):692–702. doi: 10.1042/bj0570692

Some esterases of the rat

W N Aldridge 1
PMCID: PMC1269823  PMID: 13198822

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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 properties of specific cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E 605) and analogues. Biochem J. 1950 Apr;46(4):451–460. doi: 10.1042/bj0460451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. ALDRIDGE W. N. [The inhibition of erythrocyte cholinesterase by tri-esters of phosphoric acid. III. The nature of the inhibitory process]. Biochem J. 1953 Jun;54(3):442–448. doi: 10.1042/bj0540442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. BARRNETT R. J. The distribution of esterolytic activity in the tissues of the albino rat as demonstrated with indoxyl acetate. Anat Rec. 1952 Dec;114(4):577–599. doi: 10.1002/ar.1091140405. [DOI] [PubMed] [Google Scholar]
  6. COPENHAVER J. H., STAFFORD R. O., McSHAN W. H. The determination of esterase in animal tissue homogenates. Arch Biochem. 1950 Apr;26(2):260–268. [PubMed] [Google Scholar]
  7. DAVISON A. N. Return of cholinesterase activity in the rat after inhibition by organophosphorus compounds. I. Diethyl p-nitro-phenyl phosphate (E 600, paraoxon). Biochem J. 1953 Jul;54(4):583–590. doi: 10.1042/bj0540583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. DENZ F. A. On the histochemistry of the myoneural junction. Br J Exp Pathol. 1953 Jun;34(3):329–339. [PMC free article] [PubMed] [Google Scholar]
  9. DESNUELLE P. Hydrolyse enzymatique des triglycérides. Bull Soc Chim Biol (Paris) 1951;33(8):909–923. [PubMed] [Google Scholar]
  10. Delory G. E., King E. J. The rate of enzymic hydrolysis of phosphoric esters: 2. Relation of structure to dissociation constant, Michaelis constant, and rate of hydrolysis. Biochem J. 1943;37(5):547–550. doi: 10.1042/bj0370547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. FODOR P. J. Inactivation studies on cholesterol esterase. Arch Biochem. 1950 May;26(3):331–336. [PubMed] [Google Scholar]
  12. Folley S. J., Watson S. C. A high-speed tissue homogenizer. Biochem J. 1948;42(2):204–206. doi: 10.1042/bj0420204. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. GANGULY J., DEUEL H. J., Jr Intracellular distribution of vitamin A esterase activity in rat liver. Nature. 1953 Jul 18;172(4368):120–121. doi: 10.1038/172120a0. [DOI] [PubMed] [Google Scholar]
  14. GOMORI G. Histochemical localization of true lipase. Proc Soc Exp Biol Med. 1949 Dec;72(3):697-700, illust. doi: 10.3181/00379727-72-17546. [DOI] [PubMed] [Google Scholar]
  15. KRAUSE R. F., ALBERGHINI C. The hydrolysis of vitamin A ester. Arch Biochem. 1950 Feb;25(2):396–400. [PubMed] [Google Scholar]
  16. King E. J., Delory G. E. The rates of enzymic hydrolysis of phosphoric esters. Biochem J. 1939 Aug;33(8):1185–1190. doi: 10.1042/bj0331185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. MENDEL B., MYERS D. K., UYLDERT I. E., RUYS A. C., DE BRUYN W. M. Ali-esterase inhibitors and growth. Br J Pharmacol Chemother. 1953 Jun;8(2):217–224. doi: 10.1111/j.1476-5381.1953.tb00782.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. MOUNTER L. A., WHITTAKER V. P. The hydrolysis of esters of phenol by cholinesterases and other esterases. Biochem J. 1953 Jul;54(4):551–559. doi: 10.1042/bj0540551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. MYERS D. K., MENDEL B. Studies on aliesterases and other lipid-hydrolysing enzymes. I. Inhibition of the esterases and acetoacetate production of liver. Biochem J. 1953 Jan;53(1):16–25. doi: 10.1042/bj0530016. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. McGUGAN W. A., LAUGHLAND D. H. The vitamin A esterase activity of rat liver homogenates. Arch Biochem Biophys. 1952 Feb;35(2):428–434. doi: 10.1016/s0003-9861(52)80023-2. [DOI] [PubMed] [Google Scholar]
  21. Ord M. G., Thompson R. H. The distribution of cholinesterase types in mammalian tissues. Biochem J. 1950 Mar;46(3):346–352. doi: 10.1042/bj0460346. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. REISER R., BRYSON M. J., CARR M. J., KUIKEN K. A. The intestinal absorption of triglycerides. J Biol Chem. 1952 Jan;194(1):131–138. [PubMed] [Google Scholar]
  23. REISER R., WILLIAMS M. C. Dihydroxyacetone esters as precursors of triglycerides during intestinal absorption. J Biol Chem. 1953 Jun;202(2):815–819. [PubMed] [Google Scholar]
  24. Richter D., Croft P. G. Blood esterases. Biochem J. 1942 Dec;36(10-12):746–757. doi: 10.1042/bj0360746. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. WILSON I. B., LEVINE S., FREIBERGER I. Effects of electrical charge upon the activity of liver esterase. J Biol Chem. 1952 Feb;194(2):613–617. [PubMed] [Google Scholar]

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