Human pancreatic chymotrypsinogen A: a non-competitive enzyme immunoassay, and molecular forms in serum and amniotic fluid.
Biochim Biophys Acta
; 883(1): 46-53, 1986 Aug 06.
Article
em En
| MEDLINE
| ID: mdl-3524693
ABSTRACT
A sandwich enzyme immunoassay has been developed for human pancreatic chymotrypsin(ogen) using polystyrene balls coated with specific IgG as the first antibody and peroxidase-labelled IgG as the second antibody. The detection limit was 0.5 microgram/l. A good parallelism was observed with the curves obtained from standard chymotrypsinogen A and chymotrypsin(ogen) present in pancreatic juice; however, a slight discrepancy in parallelism with chymotrypsin(ogen) present in serum and amniotic fluid was noticed. Chymotrypsinogen concentration in pancreatic juice was evaluated to represent 9% of total proteins. Mean values of chymotrypsin(ogen) in human sera were 24.6 +/- 8.3 micrograms/l in adults and 20.9 +/- 8.8 micrograms/l in newborns. In amniotic fluid at the 18th week of pregnancy the values were scattered (5-70 micrograms/l). The molecular forms of immunoreactive chymotrypsin(ogen) in normal serum and amniotic fluid have been investigated by gel filtration on Sephadex G-100. Two peaks of immunoreactive chymotrypsin(ogen) were observed in normal serum; the first peak elutes in a position consistent with a complex of chymotrypsin with serum inhibitor (Mr 76,000), and the second peak elutes with a molecular weight of approx. 25,000 corresponding to the elution position of free chymotrypsin(ogen). In normal amniotic fluid three peaks of immunoreactive material were present; the first and second peaks elute in the same position as in serum, and the third peak with a molecular weight of about 14,500 may represent a degraded form of chymotrypsin.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Suco Pancreático
/
Quimotripsinogênio
/
Líquido Amniótico
Limite:
Adult
/
Female
/
Humans
/
Newborn
/
Pregnancy
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1986
Tipo de documento:
Article