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Volumn 371, Issue 1-2, 2006, Pages 124-129

A rapid and sensitive assay for the quantitation of carboxypeptidase N, an important regulator of inflammation

Author keywords

Anaphylatoxin inactivator; Carboxypeptidase N; Inflammation; Kinetic assay

Indexed keywords

ARGININE CARBOXYPEPTIDASE; BENZOYLALANYLARGININE; BENZOYLGLYCYLARGININE; ENZYME; UNCLASSIFIED DRUG;

EID: 33746848109     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2006.02.035     Document Type: Article
Times cited : (4)

References (18)
  • 1
    • 0000077897 scopus 로고
    • An enzyme in human blood plasma that inactivates bradykinin and kallidins
    • Erdos E.G., and Sloane E.M. An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem Pharmacol 11 (1962) 562-585
    • (1962) Biochem Pharmacol , vol.11 , pp. 562-585
    • Erdos, E.G.1    Sloane, E.M.2
  • 2
    • 0346849668 scopus 로고    scopus 로고
    • Carboxypeptidase N: a pleiotropic regulator of inflammation
    • Mathews K., Mueller-Ortiz S., and Wetsel R. Carboxypeptidase N: a pleiotropic regulator of inflammation. Mol Immunol 40 (2004) 785-793
    • (2004) Mol Immunol , vol.40 , pp. 785-793
    • Mathews, K.1    Mueller-Ortiz, S.2    Wetsel, R.3
  • 3
    • 0014900566 scopus 로고
    • Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase
    • Bokisch V.A., and Müller-Eberhard H.J. Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase. J Clin Invest 49 (1970) 2427-2436
    • (1970) J Clin Invest , vol.49 , pp. 2427-2436
    • Bokisch, V.A.1    Müller-Eberhard, H.J.2
  • 5
    • 0022653736 scopus 로고
    • Decreased synthesis of serum carboxypeptidase N (SCPN) in familial SCPN deficiency
    • Mathews K.P., Curd J.G., and Hughli T.E. Decreased synthesis of serum carboxypeptidase N (SCPN) in familial SCPN deficiency. J Clin Immunol 6 (1986) 87-91
    • (1986) J Clin Immunol , vol.6 , pp. 87-91
    • Mathews, K.P.1    Curd, J.G.2    Hughli, T.E.3
  • 6
    • 0037275693 scopus 로고    scopus 로고
    • DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency
    • Cao H., and Hegele R.A. DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency. J Hum Genet 48 (2003) 20-22
    • (2003) J Hum Genet , vol.48 , pp. 20-22
    • Cao, H.1    Hegele, R.A.2
  • 7
    • 20444383082 scopus 로고    scopus 로고
    • Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell derived factor-1 alpha in the circulation
    • Davis D.A., Singer K.E., De La Luz Sierra M., et al. Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell derived factor-1 alpha in the circulation. Blood 105 (2005) 4561-4568
    • (2005) Blood , vol.105 , pp. 4561-4568
    • Davis, D.A.1    Singer, K.E.2    De La Luz Sierra, M.3
  • 8
    • 0028222563 scopus 로고
    • Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen
    • Wang W., Hendriks D.F., and Scharpé S.S. Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J Biol Chem 269 (1994) 15937-15944
    • (1994) J Biol Chem , vol.269 , pp. 15937-15944
    • Wang, W.1    Hendriks, D.F.2    Scharpé, S.S.3
  • 9
    • 15544373731 scopus 로고    scopus 로고
    • Development of a fast kinetic method for the determination of carboxypeptidase U (TAFIa) using C-terminal arginine containing peptides as substrate
    • Willemse J., Leurs J., Verkerk R., and Hendriks D. Development of a fast kinetic method for the determination of carboxypeptidase U (TAFIa) using C-terminal arginine containing peptides as substrate. Anal Biochem 340 (2005) 106-112
    • (2005) Anal Biochem , vol.340 , pp. 106-112
    • Willemse, J.1    Leurs, J.2    Verkerk, R.3    Hendriks, D.4
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-258
    • (1976) Anal Biochem , vol.72 , pp. 248-258
    • Bradford, M.1
  • 11
    • 0022248719 scopus 로고
    • Assay of carboxypeptidase N activity in serum by liquid chromatographic detection of hippuric acid
    • Hendriks D., Scharpé S., and van Sande M. Assay of carboxypeptidase N activity in serum by liquid chromatographic detection of hippuric acid. Clin Chem 12 (1985) 1936-1939
    • (1985) Clin Chem , vol.12 , pp. 1936-1939
    • Hendriks, D.1    Scharpé, S.2    van Sande, M.3
  • 12
    • 0022486640 scopus 로고
    • Colorimetric assay for carboxypeptidase N in serum
    • Hendriks D., Van Sande M., and Scharpé S. Colorimetric assay for carboxypeptidase N in serum. Clin Chim Acta 157 (1986) 103-108
    • (1986) Clin Chim Acta , vol.157 , pp. 103-108
    • Hendriks, D.1    Van Sande, M.2    Scharpé, S.3
  • 13
    • 28444441566 scopus 로고    scopus 로고
    • Fast kinetic assay for the determination of procarboxypeptidase U (TAFI) in human plasma
    • Willemse J.L., Leurs J.R., and Hendriks D.F. Fast kinetic assay for the determination of procarboxypeptidase U (TAFI) in human plasma. J Thromb Haemost 3 (2005) 2353-2355
    • (2005) J Thromb Haemost , vol.3 , pp. 2353-2355
    • Willemse, J.L.1    Leurs, J.R.2    Hendriks, D.F.3
  • 14
    • 29744453508 scopus 로고    scopus 로고
    • Measurement of procarboxypeptidase U (TAFI) in human plasma: a laboratory challenge
    • Willemse J., and Hendriks D. Measurement of procarboxypeptidase U (TAFI) in human plasma: a laboratory challenge. Clin Chem 52 (2006) 30-36
    • (2006) Clin Chem , vol.52 , pp. 30-36
    • Willemse, J.1    Hendriks, D.2
  • 15
    • 0024558753 scopus 로고
    • A labile enzyme in fresh human serum interferes with the assay of carboxypeptidase N
    • Hendriks D., Scharpé S., van Sande M., and Lommaert M.P. A labile enzyme in fresh human serum interferes with the assay of carboxypeptidase N. Clin Chem 35 (1989) 177
    • (1989) Clin Chem , vol.35 , pp. 177
    • Hendriks, D.1    Scharpé, S.2    van Sande, M.3    Lommaert, M.P.4
  • 17
    • 0031915389 scopus 로고    scopus 로고
    • Plasma and recombinant thrombin activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin dependent activation, thermal stability and enzymatic properties
    • Boffa M.B., Wang W., Bajzar L., and Nesheim M.E. Plasma and recombinant thrombin activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin dependent activation, thermal stability and enzymatic properties. J Biol Chem 273 (1998) 2127-2135
    • (1998) J Biol Chem , vol.273 , pp. 2127-2135
    • Boffa, M.B.1    Wang, W.2    Bajzar, L.3    Nesheim, M.E.4
  • 18
    • 0037059828 scopus 로고    scopus 로고
    • Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme
    • Schneider M., Boffa M., Stewart R., Rahman M., Koschinsky M., and Nesheim M. Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme. J Biol Chem 277 (2002) 1021-1030
    • (2002) J Biol Chem , vol.277 , pp. 1021-1030
    • Schneider, M.1    Boffa, M.2    Stewart, R.3    Rahman, M.4    Koschinsky, M.5    Nesheim, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.