Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1962 May;83(2):274–283. doi: 10.1042/bj0830274

Neutral proteinases in the lens

S G Waley 1, Ruth Van Heyningen 1
PMCID: PMC1243545  PMID: 14004547

Full text

PDF
277

Selected References

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

  1. ADAMS E., SMITH E. L. Proteolytic activity of pituitary extracts. J Biol Chem. 1951 Aug;191(2):651–664. [PubMed] [Google Scholar]
  2. ANSELL G. B., RICHTER D. Evidence for a neutral proteinase in brain tissue. Biochim Biophys Acta. 1954 Jan;13(1):92–97. doi: 10.1016/0006-3002(54)90276-0. [DOI] [PubMed] [Google Scholar]
  3. BODE F. Eine Vereinfachung und Verbesserung der Methode zur quantitativen Bestimmung von Aminosäuren und Peptiden mittels des Ninhydrin-Kupferkomplexes. Biochem Z. 1955;326(6):433–435. [PubMed] [Google Scholar]
  4. CLIFFE E. E., WALEY S. G. Acidic peptides of the lens. 4. The biosynthesis of ophthalmic acid. Biochem J. 1958 Aug;69(4):649–655. doi: 10.1042/bj0690649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. DANNENBERG A. M., Jr, SMITH E. L. Proteolytic enzymes of lung. J Biol Chem. 1955 Jul;215(1):45–54. [PubMed] [Google Scholar]
  6. DAVIE E. W., NEWMAN C. R., WILCOX P. E. Action of carboxypeptidase on beta-lactoglobulin. J Biol Chem. 1959 Oct;234:2635–2641. [PubMed] [Google Scholar]
  7. DEVI A., FRIEL R., LERMAN S. The RNA content and the amino acid-RNA incorporating system in the lenses of various species. Arch Ophthalmol. 1961 Jun;65:855–858. doi: 10.1001/archopht.1961.01840020857021. [DOI] [PubMed] [Google Scholar]
  8. DISCHE Z., DEVI A., ZELMENIS G. Influence of age and cataract formation on the ribonucleic acid of the lens. I. Changes in various fractions of ribonucleic acid of rat lenses during aging. Am J Ophthalmol. 1961 May;51:993–1004. doi: 10.1016/0002-9394(61)91785-8. [DOI] [PubMed] [Google Scholar]
  9. FERRINI U., ZITO R. Action of trypsin on Bence-Jones protein derivatives. Nature. 1961 Feb 11;189:485–485. doi: 10.1038/189485a0. [DOI] [PubMed] [Google Scholar]
  10. FITTKAU S., GLAESSER D., HANSON H. [On the activity and specificity of leucine aminopeptidase in eye lenses. Amino acid and dipeptide anilides as substrates]. Hoppe Seylers Z Physiol Chem. 1960 Dec 31;322:101–111. doi: 10.1515/bchm2.1960.322.1.101. [DOI] [PubMed] [Google Scholar]
  11. FRANCOIS J., RABAEY M., WIEME R. J. New method for fractionation of lens proteins. AMA Arch Ophthalmol. 1954 Apr;53(4):481–486. doi: 10.1001/archopht.1955.00930010483004. [DOI] [PubMed] [Google Scholar]
  12. FROMAGEOT P., SIRCHIS J. Isolement d'une fraction homogène de l'albumoïde du cristallin de boeuf. C R Hebd Seances Acad Sci. 1955 Apr 25;240(17):1730–1732. [PubMed] [Google Scholar]
  13. HANSON H., KLEINE R., BLECH W. [The decomposition of cathepsin C- and chymotrypsin-substrates as well as hemoglobin by animal organs and their cell components]. Hoppe Seylers Z Physiol Chem. 1959 Oct 30;316:127–136. doi: 10.1515/bchm2.1959.316.1.127. [DOI] [PubMed] [Google Scholar]
  14. HANSON H., METHFESSEL J. Zur Spezifität der Peptidaseaktivivität der Rinderlinse. Acta Biol Med Ger. 1958;1(4):414–421. [PubMed] [Google Scholar]
  15. HILL R. L., SMITH E. L. Leucine aminopeptidase. VII. Action on long chain polypeptides and proteins. J Biol Chem. 1957 Oct;228(2):577–600. [PubMed] [Google Scholar]
  16. KORNER A., TARVER H. Studies on protein synthesis in vitro. VI. Incorporation and release of amino acids in particulate preparations from livers of rats. J Gen Physiol. 1957 Sep 20;41(1):219–231. doi: 10.1085/jgp.41.1.219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. KOSZALKA T. R., MILLER L. L. Proteolytic activity of rat skeletal muscle. I. Evidence for the existence of an enzyme active optimally at pH 8.5 to 9.0. J Biol Chem. 1960 Mar;235:665–668. [PubMed] [Google Scholar]
  18. KOSZALKA T. R., MILLER L. L. Proteolytic activity of rat skeletal muscle. II. Purification and properties of an enzyme active optimally at pH 8.5 to 9.0. J Biol Chem. 1960 Mar;235:669–672. [PubMed] [Google Scholar]
  19. LAPRESLE C., WEBB T. Study of a proteolytic enzyme from rabbit spleen. Biochem J. 1960 Sep;76:538–543. doi: 10.1042/bj0760538. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. MANDEL P., DARDENNE U., LESSINGER A. Incorporation et dégradation de la méthionine par le cristallin de bovidés. C R Hebd Seances Acad Sci. 1957 Sep 9;245(11):985–987. [PubMed] [Google Scholar]
  21. MARTIN C. J., AXELROD A. E. The proteolytic enzyme system of skin. III. Purification of proteinase C and its separation from an inhibitor. Biochim Biophys Acta. 1958 Jan;27(1):52–62. doi: 10.1016/0006-3002(58)90292-0. [DOI] [PubMed] [Google Scholar]
  22. MATHESON A. T., TIGANE E., HANES C. S. Quantitative chromatographic methods. 5. An improved ninhydrin-hydrindantin reagent. Can J Biochem Physiol. 1961 Feb;39:417–425. doi: 10.1139/o61-040. [DOI] [PubMed] [Google Scholar]
  23. MERRIAM F. C., KINSEY V. E. Studies on the crystalline lens. III. Incorporation of glycine and serine in the proteins of lenses cultured in vitro. AMA Arch Ophthalmol. 1950 Nov;44(5):651–658. [PubMed] [Google Scholar]
  24. MEYER H. The ninhydrin reaction and its analytical applications. Biochem J. 1957 Oct;67(2):333–340. doi: 10.1042/bj0670333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. MOORE S., STEIN W. H. A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. J Biol Chem. 1954 Dec;211(2):907–913. [PubMed] [Google Scholar]
  26. MORRISON W. L., NEURATH H. Proteolytic enzymes of the formed elements of human blood. I. Erythrocytes. J Biol Chem. 1953 Jan;200(1):39–51. [PubMed] [Google Scholar]
  27. PATTERSON E. K. Leucine aminopeptidase fragments from an ascites tumor. J Biol Chem. 1959 Sep;234:2327–2336. [PubMed] [Google Scholar]
  28. PHILLIPS D. M., JOHNS E. W. A study of the proteinase content and the chromatography of thymus histones. Biochem J. 1959 Jul;72:538–544. doi: 10.1042/bj0720538. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. PIEZ K. A., OYAMA V. I., LEVINTOW L., EAGLE H. Proteolysis in stored serum and its possible significance in cell culture. Nature. 1960 Oct 1;188:59–60. doi: 10.1038/188059a0. [DOI] [PubMed] [Google Scholar]
  30. PORCELLATI G., CURTI B. Proteinase activity of peripheral nerves during Wallerian degeneration. J Neurochem. 1960 May;5:277–282. doi: 10.1111/j.1471-4159.1960.tb13364.x. [DOI] [PubMed] [Google Scholar]
  31. PRESS E. M., PORTER R. R., CEBRA J. The isolation and properties of a proteolytic enzyme, cathepsin D, from bovine spleen. Biochem J. 1960 Mar;74:501–514. doi: 10.1042/bj0740501. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. SIMKIN J. L. Protein biosynthesis. Annu Rev Biochem. 1959;28:145–170. doi: 10.1146/annurev.bi.28.070159.001045. [DOI] [PubMed] [Google Scholar]
  33. STEINBERG D., VAUGHAN M. Observations on intracellular protein catabolism studied in vitro. Arch Biochem Biophys. 1956 Nov;65(1):93–105. doi: 10.1016/0003-9861(56)90180-1. [DOI] [PubMed] [Google Scholar]
  34. TODD P. E., TRIKOJUS V. M. Purification and properties of adrenal acid proteinase. Biochim Biophys Acta. 1960 Dec;45:234–242. doi: 10.1016/0006-3002(60)91447-5. [DOI] [PubMed] [Google Scholar]
  35. TROLL W., CANNAN R. K. A modified photometric ninhydrin method for the analysis of amino and imino acids. J Biol Chem. 1953 Feb;200(2):803–811. [PubMed] [Google Scholar]
  36. WILLIAMS W. J., THORNE C. B. Biosynthesis of glutamyl peptides from glutamine by a transfer reaction. J Biol Chem. 1954 Sep;210(1):203–217. [PubMed] [Google Scholar]
  37. ZELLER E. A., SHOCH D. On the enzymology of the refractory media of the eye. VI. Effect of intralenticular injection of halogen acetates on the transparency and peptidase activity of the rabbit lens. Am J Ophthalmol. 1961 Jul;52:65–72. [PubMed] [Google Scholar]

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

RESOURCES