Human oviductal fluid proteins. V. Identification of human oviductin-I as alpha-fetoprotein
Autor: | Jack Lippes, Premanand V. Wagh |
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Rok vydání: | 1993 |
Předmět: |
medicine.drug_class
Size-exclusion chromatography Blotting Western Radioimmunoassay Enzyme-Linked Immunosorbent Assay Monoclonal antibody Immunoglobulin G Immunochemistry medicine Animals Humans Fallopian Tubes Serum Albumin Glycoproteins chemistry.chemical_classification biology Molecular mass Obstetrics and Gynecology Proteins Amino acid Body Fluids Reproductive Medicine chemistry Biochemistry Polyclonal antibodies biology.protein Electrophoresis Polyacrylamide Gel Female alpha-Fetoproteins Alpha-fetoprotein |
Zdroj: | Fertility and sterility. 59(1) |
ISSN: | 0015-0282 |
Popis: | Objective To investigate whether human oviductin-I (hOV-I) from human oviductal fluid (hOF) and human alpha-fetoprotein (hAFP) are identical molecules. Design Comparison of amino acid and carbohydrate composition of hOV-I with that of hAFP. Isolation of hAFP from oviductal fluid of a patient and evaluation of its immunochemical properties in relation to hOV-I and authentic hAFP standard. Setting Procedures were performed in an academic research environment. Patients Human oviductin-I was isolated from a pooled sample of hOF obtained from four patients in a third world country. AFP was purified from a sample of oviductal fluid obtained from a single patient during her periovulatory period. Interventions Human oviductal fluid was collected coincident to elective tubal ligations. Main Outcome Measures The amino acid and carbohydrate composition of hOV-I was determined. AFP was purified from hOF using ion-exchange chromatography and gel filtration. The identity between hOV-I and hAFP from hOF was assessed using enzyme-linked immunosorbent assay (ELISA) and Western immunoblot analysis. Results The amino acid and carbohydrate composition of hOV-I indicated similarities between hOV-I and hAFP. Both hOV-I and hAFP reacted with mouse anti-hAFP monoclonal antibody and purified polyclonal rabbit anti-hOV-I immunoglobulin G in an identical manner as observed by noncompetitive ELISA. Purified AFP from hOF of a single patient had a molecular mass of 66 kd and was found to be identical with hOV-I by Western immunoblot analysis. Conclusions Human oviductin-I and hAFP are chemically similar and immunologically identical molecules. We believe that this finding is the first documentation for the existence of AFP in hOF. |
Databáze: | OpenAIRE |
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