Human oviductal fluid proteins. V. Identification of human oviductin-I as alpha-fetoprotein.

Fertil Steril

Department of Biochemical Pharmacology, School of Pharmacy, State University of New York, Buffalo.

Published: January 1993

AI Article Synopsis

  • The study aimed to determine if human oviductin-I (hOV-I) and human alpha-fetoprotein (hAFP) are the same substance by comparing their amino acid and carbohydrate structures.
  • Procedures involved isolating hAFP from the oviductal fluid of a patient, while hOV-I was obtained from pooled samples of several patients.
  • Results showed that hOV-I and hAFP have similar chemical compositions and reacted the same in various immunological tests, suggesting they are identical molecules and marking the first evidence of AFP presence in human oviductal fluid.

Article Abstract

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.

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http://dx.doi.org/10.1016/s0015-0282(16)55631-3DOI Listing

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