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Biology of Reproduction 63, 30-33 (2000)
© 2000 Society for the Study of Reproduction, Inc.


Regular Article

Purification, Characterization, and Biological Compartmentalization of Rat Fetal Antigen 11

Hans-Erik Carlsson2,,a, Gabriella Persdotter-Hedlunda, Erik Friesb, Ulf J. Erikssonc, and Jann Haua

a Department of Physiology, b Division of Comparative Medicine, Department of Medical Biochemistry and Microbiology, c Section of Medical Biochemistry, and Department of Medical Cell Biology, Uppsala University, 751 23 Uppsala, Sweden

ABSTRACT

This study has established the rat as an animal model for the analysis of the biological role of fetal antigen 1 (FA1), a protein previously described in humans and mice. FA1 was purified from rat amniotic fluid by immunospecific affinity chromatography. Immunochemical identity between mouse and rat FA1 was established by crossed tandem immunoelectrophoresis. Molecular size was analyzed by mass spectrometry (33 kDa). The amino acid composition was determined, and the amino acid sequence was analyzed. The overall amino acid composition and sequence of the 28 first N-terminal amino acids were identical to the corresponding parts of rat preadipocyte factor 1 and rat adrenal zona glomerulosa protein. Extensive sequence similarity was found between rat and mouse FA1 (86%) and between rat and human FA1 (82%). The concentration of FA1 in fetal serum, maternal serum, urine, and amniotic fluid in rats was determined using an ELISA. The highest concentrations were found in fetal serum and amniotic fluid around Day 18 of pregnancy. This is the first report on the physicochemical characteristics and compartmentalization of rat FA1.

FOOTNOTES

First decision: 17 September 1999.

1 This work was supported by the Swedish Medical Research Council, projects 12567 and 7475.

2 Correspondence: Hans-Erik Carlsson, Department of Physiology, Division of Comparative Medicine, Box 572, Uppsala University, SE-751 23 Uppsala, Sweden. FAX: 46 18 501740; hans-erik.carlsson{at}bmc.uu.se







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