ABSTRACT
The presence of amylase in normal and neoplastic salivary gland tissue was investigated by immunoperoxidase techniques. Apart from normal and inflamed parotid glands, different kinds of tumours were studied with regard to amylase: acinic cell tumours, adenocarcinomas, adenoidcystic carcinomas, salivary duct carcinomas, mucoepidermoid tumours and squamous cell carcinomas. Amylase could be seen in acinic cell tumours, but not in other neoplasms. The results were discussed with respect to the diagnostic implications.
Subject(s)
Amylases/analysis , Salivary Gland Neoplasms/enzymology , alpha-Amylases/analysis , Adenocarcinoma/enzymology , Carcinoma/enzymology , Carcinoma, Adenoid Cystic/enzymology , Carcinoma, Intraductal, Noninfiltrating/enzymology , Carcinoma, Squamous Cell/enzymology , Humans , Immunoenzyme Techniques , Parotid Gland/enzymology , Parotitis/enzymologyABSTRACT
A highly sensitive and specific enzyme immunoassay for the determination of pancreatic lipase is described. The test follows the sandwich principle; total incubation time is 4.5 hours at 20--25 degrees C. Lipase concentrations between 3 and 300 micrograms/1 can be quantified (sample dilution 1 + 10); the lower detection limit is 0.3 micrograms/1 (sample dilution 1 + 1). Coefficients of variation from 2.9 to 6.5% for the in batch precision, and from 4.4 to 10.5% for the day-to day precision were found. A reference range from 7.7 to 56 micrograms/1 was calculated from the lipase concentrations in 369 serum samples from healthy adults (2.5 th--97.5 th percentile, median 23 micrograms/1). Very low concentrations were found in cord blood (median 2.8 micrograms/1). The lipase level remains quite constant between the ages of 3 and 50 years (median 15--20 micrograms/1); at the age of 70 years a median of 26 micrograms/1 is reached.
Subject(s)
Immunoenzyme Techniques , Lipase/blood , Pancreas/enzymology , Adolescent , Adult , Aged , Aging , Child , Child, Preschool , Fetal Blood/enzymology , Humans , Immunoenzyme Techniques/standards , Middle Aged , Reference ValuesSubject(s)
Antibody-Dependent Cell Cytotoxicity , Lymphocytes/immunology , Neuraminidase/pharmacology , Adolescent , Adult , Aged , Antibodies/isolation & purification , Antibody Specificity , Antibody-Dependent Cell Cytotoxicity/drug effects , Complement System Proteins , Galactose/pharmacology , Hemagglutination , Humans , Immunosorbent Techniques , In Vitro Techniques , Infant, Newborn , Influenza Vaccines/pharmacology , Lactose/pharmacology , Middle AgedABSTRACT
Purification of human pregnancy-specific beta1-glycoprotein (SP1) and antigenically related proteins of sub-human primates (chimpanzee, rhesus monkey, cynomolgus and baboon) was achieved by means of an immunoadsorbent technique. The immunoglobulins of a rabbit antiserum to human SP1 were isolated on DEAE-cellulose and coupled to CNBr-activated Sepharose. This immunoadsorbent was used to bind human SP1, respectively monkey proteins immunochemically related to SP1 from placental extract fractions. After extensive washing the proteins were eluted by an acidic glycine buffer. Contaminating serum proteins could be removed by chromatography on hydroxyapatite columns. With this method it was possible to obtain SP1 and the antigenically related proteins of monkeys in good yield and in highly purified form. The proteins thus isolated from human and sub-human primate placentae were compared in their physicochemical and immunochemical properties. The amino acid and carbohydrate compositions of human SP1 and rhesus SP1 have been determined. In a biological test certain inhibitory effect of human SP1 on the mixed leukozyte culture (MLC) could be demonstrated.
