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Preparation of di peptidylamino peptidase iv ec 3.4.14. for poly peptide sequencing


, : Preparation of di peptidylamino peptidase iv ec 3.4.14. for poly peptide sequencing. Biochimica et Biophysica Acta 576(2): 280-289

Dipeptidyl aminopeptidase IV is a dipeptidylpeptide hydrolase (EC 3.4.14) which hydrolyzes bonds at the carboxyl group of proline releasing X-Pro dipeptides from the amino-terminus of polypeptides. The enzyme was purified 440-fold in 37% yield from swine kidney by ammonium sulfate fractionation, DEAE-cellulose chromatography, gel filtration and affinity chromatography with dipeptide-substituted Sepharose 4B. The enzyme released X-Pro from all X-Pro-.beta.-naphthylamides and polypeptides tested. The released dipepeptides were not further degraded, and were readily identified in digests. The enzyme is suitable for use in the dipeptidyl aminopeptidase method for polypeptide sequence analysis.


Accession: 006173049

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Related references

Sutherland D.E., 1973: Poly peptide sequencing use of di peptidylamino peptidase i and gas chromatography mass spectrometry. Biochemical & Biophysical Research Communications: 67-75

Anonymous, 1972: Water insoluble enzymes for peptide sequencing di peptidylamino peptidase i cathepsin c ec 3449 an enzyme with subunit structure

Krutzsch H.C.; Pisano J.J., 1975: Use of di peptidylamino peptidases with gas chromatography mass spectroscopy in poly peptide sequencing. Federation Proceedings 34(3): 630

Yoshimoto, T.; Walter, R., 1977: Post proline di peptidylamino peptidase ec 3.4.14.1 di peptidylamino peptidase iv from lamb kidney purification and some enzymatic properties. Post-proline dipeptidyl aminopeptidase (dipeptidylpeptide hydrolase, EC 3.4.14.1), also known as glycylprolyl .beta.-naphthylamidase or dipeptidyl aminopeptidase IV, was isolated and purified in an overall yield of 20% from autolyzed extracts of l...

Lindley, H.; Rowlands, R.J., 1972: The specificity of di peptidylamino peptidase i cathepsin c and its use in peptide sequence studies. Biochemical Journal 126(3): 683-688

Caprioli R.M.; Seifert W.E., 1975: Hydrolysis of poly peptides and proteins utilizing a mixture of di peptidylamino peptidase with analysis by gas chromatography mass spectrometry. Biochemical & Biophysical Research Communications 64(1): 295-303

Auricchio, S.; Greco, L.; De-Vizia, B.; Buonocore, V., 1978: Di peptidylamino peptidase and carboxy peptidase activities of the brush border of rabbit small intestine. Two peptidases were found in the brush border of rabbit small intestine: dipeptidylaminopeptidase IV, which is able to hydrolyze glycyl-L-proline from glycyl-L-prolyl-.beta.-naphthylamide, and a carboxypeptidase, which is able to hydrolyze N-carbo...

Swanson, A.A.; Albers-Jackson, B.; Mcdonald, J.K., 1978: Mammalian lens di peptidylamino peptidase iii ec 3.1.14.. An intracellular exopeptidase identified as dipeptidyl aminopeptidase III (DAP III) (EC-3.4.14.-) was abundant in the bovine lens. The enzyme contained in aqueous extracts exhibited a marked preference, compared to other dipeptidyl-.beta.-naphthyl...

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Metrione, R.M., 1978: Chromatography of di peptidylamino peptidase i ec 3.4.14.1 on inhibitor sepharose columns. A number of affinity materials for the purification of dipeptidyl aminopeptidase (dipeptidylpeptide hydrolase, EC 3.4.14.1) were prepared and tested. These materials include peptide and amino acid inhibitors bound to agarose and reversible sulfhyd...