EurekaMag.com logo
+ Translate

The primary structure of leucine amino peptidase ec 3.4.11.1 from bovine eye lens


, : The primary structure of leucine amino peptidase ec 3.4.11.1 from bovine eye lens. Journal of Biological Chemistry 257(12): 7077-7085

The amino acid sequence of bovine eye lens leucine aminopeptidase was determined. Cyanogen bromide fragments, the COOH-terminal hydroxylamine fragment and a large fragment obtained by digestion with Staphylococcus aureus protease were isolated from reduced and S-alkylated leucine aminopeptidase. The amino acid sequences of these fragments were determined by automated sequence analysis, by manual direct Edman degradation and by the dansyl-Edman technique. Overlapping peptides were obtained by tryptic digestion of the S-alkylated protein or the citraconylated S-alkylated protein. The polypeptide chain of leucine aminopeptidase comprises 478 residues, corresponding to a MW of 51,691. No significant sequence homology with any other published protein primary structure could be detected. This is the 1st report of a complete amino acid sequence of an enzyme belonging to the class of 2-metal peptidases.

(PDF 0-2 workdays service)

Accession: 006740933

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Van-Loon-Klaassen, L.A.H.; Cuypers, H.T.; Van-Westreenen, H.; De-Jong, W.W.; Bloemendal, H., 1980: The primary structure of bovine lens leucine amino peptidase ec 3.4.11.1 complete amino acid sequence of the amino terminal cyanogen bromide fragment and site of limited tryptic digestion. The amino acid sequence of the N-terminal cyanogen bromide fragment of bovine lens leucine aminopeptidase was determined. This fragment contains 171 amino acid residues and has a calculated MW of 18,637. The sequence data presented here represent...

Taylor A.; Daims M.; Lee J.; Surgenor T., 1983: Identification and quantification of leucine amino peptidase in aged normal and cataractous human lenses and ability of bovine lens leucine amino peptidase to cleave bovine crystallins. Rabbit antisera to bovine lens leucine amino-peptidase (LAP) were prepared. These LAP-specific antisera cross-react with a component, LAP, in human lens homogenates. Bovine and human lens LAP are similar but not identical. Immunodiffusion tests sh...

Thompson, G.A.; Carpenter, F.H., 1976: Leucine amino peptidase ec 3.4.1.1 bovine lens the relative binding of cobalt and zinc to leucine amino peptidase and the effect of cobalt substitution on specific activity. Journal of Biological Chemistry 251(6): 1618-1624

Anonymous, 1981: Comparison of bovine lens and hog lens leucine amino peptidase ec 34111 by micro complement fixation

Frohne M.; Hanson H., 1969: Studies on the structure and enzymatic activity of enz leucine amino peptidase from bovine lens in solutions containing urea guanidine hydro chloride and sodium dodecyl sulfate. Z Physiol Chem 350(2): 207-212

Kettmann U.; Kretschmer K.; Hanson H., 1968: Crystalline enz leucine amino peptidase from bovine lens amino acid composition and nitrogen terminal amino acids pig kidney. Z Physiol Chem 349(11): 1537-1542

Lasch J., 1979: Kinetic properties of bovine lens leucine amino peptidase. Ophthalmic Research 11(5-6): 372-376

Anonymous, 1975: Metal ion activation of leucine amino peptidase ec 3411 bovine lens

Taylor, A.; Carpenter, F.H.; Wlodawer, A., 1979: Leucine amino peptidase ec 3.4.11.1 bovine lens an electron microscopic study. The quaternary structure of leucine aminopeptidase (EC 3.4.11.1) was studied by EM of negatively stained single molecules and of stained and unstained thin sections of crystals. The predominant images observed in micrographs of single molecules we...

Melbye, S.W.; Carpenter, F.H., 1971: Leucine amino peptidase ec 3.4.1.1 bovine lens stability and size of subunits. Journal of Biological Chemistry 246(8): 2459-2463