Purification, characterization, and biological compartmentalization of rat fetal antigen
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Purification, characterization, and biological compartmentalization of rat fetal antigen. / Carlsson, Hans Erik; Persdotter-Hedlund, Gabriella; Fries, Erik; Eriksson, Ulf J.; Hau, Jann.
In: Biology of Reproduction, Vol. 63, No. 1, 2000, p. 30-33.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Purification, characterization, and biological compartmentalization of rat fetal antigen
AU - Carlsson, Hans Erik
AU - Persdotter-Hedlund, Gabriella
AU - Fries, Erik
AU - Eriksson, Ulf J.
AU - Hau, Jann
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
KW - Conceptus
KW - Developmental biology
KW - Pregnancy
UR - http://www.scopus.com/inward/record.url?scp=0033918372&partnerID=8YFLogxK
U2 - 10.1095/biolreprod63.1.30
DO - 10.1095/biolreprod63.1.30
M3 - Journal article
C2 - 10859238
AN - SCOPUS:0033918372
VL - 63
SP - 30
EP - 33
JO - Biology of Reproduction
JF - Biology of Reproduction
SN - 0006-3363
IS - 1
ER -
ID: 369372222