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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 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. Biochemical and Biophysical Research Communications 95(1): 334-341

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 the first report of primary structure determination of a member of the class of aminopeptidases. The single cleavage site produced by limited tryptic digestion of native leucine aminopeptidase was between Arg-137 and Lys-138 of the total amino acid sequence. The possible existence of distinct structural domains in leucine aminopeptidase is discussed.

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Related references

van Loon-Klaassen, L.A.; Cuypers, H.T.; van Westreenen, H.; de Jong, W.W.; Bloemendal, H., 1980: The primary structure of bovine lens leucine aminopeptidase. Complete amino acid sequence of the N-terminal cyanogen bromide fragment and site of limited tryptic digestion. Biochemical and Biophysical Research Communications 95(1): 334-341

Chashchin, V.L.; Lapko, V.N.; Adamovich, T.B.; Lapko, A.G.; Kuprina, N.S.; Kirillova, N.M.; Berikbaeva, T.M.; Akhrem, A.A.; Zolotarev, A.S., 1985: Primary structure of 20s 22r cholesterol hydroxylating cytochrome p 450 from bovine adrenal cortex mitochondria iv. structural investigation of thermolytic and limited tryptic hydrolysis of fragment f 1 cyanogen bromide peptides of cytochrome p 450 complete amino acid sequence. A thermolytic hydrolysis of maleinated fragment F1 has been performed, resulted in isolation of 44 peptides; their complete amino acid sequence has been determined. Non-overlapping thermolytic peptides of fragment F1 involve 178 amino acid residue...

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Bradshaw R.A.; Babin D.R.; Nomoto M.; Srinivasin N.G.; Ericsson L.H.; Walsh K.A.; Neurath H., 1969: The amino acid sequence of bovine carboxy peptidase a part 2 tryptic and chymotryptic peptides of the cyanogen bromide fragment f iii. Biochemistry 8(9): 3859-3871

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Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Mortenson, L.E., 1977: The amino acid sequence of clostridium pasteurianum iron protein a component of nitrogenase part 3 the amino terminal and carboxyl terminal sequences tryptic peptides of large cyanogen bromide peptides and the complete sequence. A total of 27 tryptic peptides were isolated from 3 large CNBr peptides (B3, B7 and B8) made from the Fe protein of nitrogenase (Fe protein(N2)). Sequence studies of these tryptic peptides verified the previously determined sequences of the 3 CNBr...

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Lai C.Y., 1975: Studies on the structure of rabbit muscle aldolase ec 41213 ordering of the tryptic peptides sequence of 164 amino acid residues in the amino terminal cyanogen bromide peptide. Archives Of Biochemistry & Biophysics: 347-357

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

Bradshaw, R.A.; Babin, D.R.; Nomoto, M.; Srinivasin, N.G.; Ericsson, L.H.; Walsh, K.A.; Neurath, H., 1969: The amino acid sequence of bovine carboxypeptidase A. II. Tryptic and chymotryptic peptides of the cyanogen bromide fragment F-III. Biochemistry 8(9): 3859-3871