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Volumn 524, Issue , 2003, Pages 57-63

The specificity of DP IV for natural substrates is peptide structure determined

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; GLUCAGON LIKE PEPTIDE 1;

EID: 0037687917     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (9)

References (8)
  • 1
    • 0026704502 scopus 로고
    • Kinetics of dipeptidyl peptidase IV proteolysis of growth hormone-releasing factor and analogs
    • Bongers, J., Lambros, T., Ahmad, M. and Heimer, E.P.; 1992, Kinetics of dipeptidyl peptidase IV proteolysis of growth hormone-releasing factor and analogs. Biochim. Biophys. Acta: 1122-147.
    • (1992) Biochim. Biophys. Acta , pp. 1122-1147
    • Bongers, J.1    Lambros, T.2    Ahmad, M.3    Heimer, E.P.4
  • 3
    • 0029118049 scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • Kieffer, T.J., McIntosh, C.H. and Pederson, R.A., 1995, Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology 136 (8): 3585-3596.
    • (1995) Endocrinology , vol.136 , Issue.8 , pp. 3585-3596
    • Kieffer, T.J.1    McIntosh, C.H.2    Pederson, R.A.3
  • 5
    • 0035798196 scopus 로고    scopus 로고
    • Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion
    • Lambeir, A.M., Durinx, C., Proost, P., Van Damme, J., Scharpé, S. and DeMeester, I., 2001, Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion. FEBS Lett. 507:327-330.
    • (2001) FEBS Lett. , vol.507 , pp. 327-330
    • Lambeir, A.M.1    Durinx, C.2    Proost, P.3    Van Damme, J.4    Scharpé, S.5    DeMeester, I.6
  • 6
    • 0027215348 scopus 로고
    • Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein, R., Gallwitz, B. and Schmidt, W.E., 1993, Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur J Biochem 214:829-835.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 7
    • 0028953577 scopus 로고
    • Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo
    • Deacon, C.F., Johnsen, A.H. and Holst, J.J., 1995, Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo. J.Clin.Endocrinol.Metab 80:952-957.
    • (1995) J.Clin.Endocrinol.Metab. , vol.80 , pp. 952-957
    • Deacon, C.F.1    Johnsen, A.H.2    Holst, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.