Ocular aminopeptidase activity and distribution in the albino rabbit
- 1 January 1985
- journal article
- research article
- Published by Taylor & Francis in Current Eye Research
- Vol. 4 (9) , 995-1000
- https://doi.org/10.3109/02713689509000007
Abstract
Ocular aminopeptidase activity in the albino rabbit was determined using L-leucine-, L-alanine-, and L-arginine-4-methoxy-2-naphthylamide as substrates. The corneal epithelium and the irisciliary body were found to be the most active, followed by, in turn, conjunctiva and corneal stroma, lens and aqueous humor, and lastly tears. The pattern of substrate hydrolysis suggests that a common dominant aminopeptidase is present in these tissues except the conjunctiva. While the role of these peptidases in ocular physiology is unknown, they may play a role in limiting the entry of topically applied peptides into the eye.Keywords
This publication has 15 references indexed in Scilit:
- Autacoids and NeuropeptidesPublished by Springer Nature ,1984
- Soluble exopeptidases of bovine and human lens: characterization by electrophoresisCurrent Eye Research, 1984
- A membrane-bound aminopeptidase isolated from monkey brain and its action on enkephalinBiochimica et Biophysica Acta (BBA) - General Subjects, 1983
- Lens exopeptidasesExperimental Eye Research, 1981
- Comparison of human membrane-bound neutral arylamidases from small intestine, lung, kidney, liver and placentaClinica Chimica Acta; International Journal of Clinical Chemistry, 1977
- Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomerArchives of Biochemistry and Biophysics, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Tissue distributions, substrate specificities and molecular sizes of human peptidases determined by separate gene lociAnnals of Human Genetics, 1971
- The hydrolysis of amino acyl-β-naphthylamides by plasma aminopeptidasesBiochemical and Biophysical Research Communications, 1964
- Published by Elsevier ,1963