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Volumn 272, Issue 2, 1998, Pages 137-147

Amylase measurement with 2-chloro-4-nitrophenyl maltotrioside as substrate

Author keywords

2 chloro 4 nitrophenyl maltotrioside (CNP G3); Measurement of amylase activity; Method comparison

Indexed keywords

2 CHLORO 4 NITROPHENYL MALTOTRIOSIDE; AMYLASE; REAGENT; UNCLASSIFIED DRUG;

EID: 0032571789     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-8981(98)00009-6     Document Type: Article
Times cited : (49)

References (13)
  • 1
    • 0021176306 scopus 로고
    • Diagnostic tests and procedures in acute pancreatitis
    • [1] Moosa AR. Diagnostic tests and procedures in acute pancreatitis. New Engl J Med 1984;311:639-43.
    • (1984) New Engl J Med , vol.311 , pp. 639-643
    • Moosa, A.R.1
  • 2
    • 0024816807 scopus 로고
    • Diagnostic enzymes for pancreatic disease
    • [2] Eckfeldt JH, Levitt MD. Diagnostic enzymes for pancreatic disease. Clinics Lab Med 1989;9:732-43.
    • (1989) Clinics Lab Med , vol.9 , pp. 732-743
    • Eckfeldt, J.H.1    Levitt, M.D.2
  • 3
    • 0020454937 scopus 로고
    • Mechanism of action of human pancreatic and salivary α-amylase on α-4-nitrophenyl maltoheptaoside substrate
    • [3] Hagele E-O, Schaich E, Rauscher E, Lehmann P, Burk H, Wahlefeld A-W. Mechanism of action of human pancreatic and salivary α-amylase on α-4-nitrophenyl maltoheptaoside substrate. Clin Chem 1982;28:2201-5.
    • (1982) Clin Chem , vol.28 , pp. 2201-2205
    • Hagele, E.-O.1    Schaich, E.2    Rauscher, E.3    Lehmann, P.4    Burk, H.5    Wahlefeld, A.-W.6
  • 4
    • 0025760075 scopus 로고
    • Determination of α-amylase using a new blocked substrate (3-ketobutylidene β-2-chloro-4-nitrophenyl-maltopentaoside)
    • [4] Teshima S, Hayashi Y, Emi S, Ishimaru K. Determination of α-amylase using a new blocked substrate (3-ketobutylidene β-2-chloro-4-nitrophenyl-maltopentaoside). Clin Chim Acta 1991;199:23-32.
    • (1991) Clin Chim Acta , vol.199 , pp. 23-32
    • Teshima, S.1    Hayashi, Y.2    Emi, S.3    Ishimaru, K.4
  • 5
    • 0025013878 scopus 로고
    • Advances in the enzyme diagnosis of pancreatic disease
    • [5] Schmidt E, Schmidt FW. Advances in the enzyme diagnosis of pancreatic disease. Clin Biochem 1990;23:383-94.
    • (1990) Clin Biochem , vol.23 , pp. 383-394
    • Schmidt, E.1    Schmidt, F.W.2
  • 6
    • 84941610417 scopus 로고
    • Evaluation of α-amylase assays with 4-nitrophenyl-α-oligosaccharides as substrates
    • [6] Lorentz K. Evaluation of α-amylase assays with 4-nitrophenyl-α-oligosaccharides as substrates. J Clin Chem Clin Biochem 1983;21:463-71.
    • (1983) J Clin Chem Clin Biochem , vol.21 , pp. 463-471
    • Lorentz, K.1
  • 7
    • 0028989670 scopus 로고
    • Amylase measurement - Which method
    • [7] Foo AY. Amylase measurement - which method. Ann Clin Biochem 1995;32:239-43.
    • (1995) Ann Clin Biochem , vol.32 , pp. 239-243
    • Foo, A.Y.1
  • 8
    • 0023916708 scopus 로고
    • Amylase measurement in serum - Old myths die hard
    • [8] Tietz NW. Amylase measurement in serum - old myths die hard (Editorial). J Clin Chem Clin Biochem 1988;26:251-3.
    • (1988) J Clin Chem Clin Biochem , vol.26 , pp. 251-253
    • Tietz, N.W.1
  • 10
    • 0022885477 scopus 로고
    • Graphical comparisons of interferences in clinical chemistry instrumentation
    • [10] Glick MR, Ryder KW, Jackson SA. Graphical comparisons of interferences in clinical chemistry instrumentation. Clin Chem 1986;32:470-5.
    • (1986) Clin Chem , vol.32 , pp. 470-475
    • Glick, M.R.1    Ryder, K.W.2    Jackson, S.A.3
  • 11
    • 0024542828 scopus 로고
    • Methods compared for determining total amylase activity and amylase isoenzymes in serum
    • [11] Badenoch JL, Bais R. methods compared for determining total amylase activity and amylase isoenzymes in serum. Clin Chem 1989;35:645-8.
    • (1989) Clin Chem , vol.35 , pp. 645-648
    • Badenoch, J.L.1    Bais, R.2
  • 12
    • 0000729088 scopus 로고
    • A new enzymatic kinetic method for determination of α-amylase
    • [12] Pierre KJ, Tung KK, Nadj H. A new enzymatic kinetic method for determination of α-amylase (abstract). Clin Chem 1976;22:1219.
    • (1976) Clin Chem , vol.22 , pp. 1219
    • Pierre, K.J.1    Tung, K.K.2    Nadj, H.3
  • 13
    • 0017924134 scopus 로고
    • Influence of thiocynate ions on starch-iodine reaction used for the estimation of α-amylase activity
    • [13] Lathia D, Brendebach M. Influence of thiocynate ions on starch-iodine reaction used for the estimation of α-amylase activity. Clin Chim Acta 1978;82:209-214.
    • (1978) Clin Chim Acta , vol.82 , pp. 209-214
    • Lathia, D.1    Brendebach, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.