TY - JOUR
T1 - Chemical and immunochemical studies on pregnant mare serum gonadotropin
AU - Schams, Dieter
AU - Papkoff, Harold
N1 - Funding Information:
Medical Sciences, National Institutes of Health. D.S. was supported by a fellowship from the Deutsche Forschungsgemeinschaft, German Research Foundation. We also thank Mrs. Inge Schams for invaluable assistance in these studies. It is also a pleasure to thank Dr. H. Gibian of Schering (Berlin) and Dr. J. D. H. Homan of Organon (Oss) for their generous supply of PMSG preparations.
Funding Information:
We wish to thank Professor C. H. Li for suggesting and encouraging these studies. The work was supported in part by grants from the National Institute of Arthritis and Metabolic Diseases (AM-6o97) and the National Institute of Child Health and Development (HD-o5722), National Institutes of Health. One of us (H.P.) is a Career Development Awardee of the National Institute of General
PY - 1972/3/15
Y1 - 1972/3/15
N2 - Highly purified pregnant mare serum gonadotropin (PMSG) can be prepared from crude commercial preparations of PMSG by chromatography on sulfoethyl-Sephadex C-50 and gel filtration on Sephadex G-100. The preparation was examined by disc electrophoresis and gel filtration and found to be of high purity. Amino acid analysis shows similarities to pituitary gonadotropins. The PMSG contains a high content of proline and cystine and low amounts of the aromatic amino acids. Phenylalanine is the major amino terminal amino acid. The carbohydrate content totals 45% of which 10% is the content of sialic acid. The PMSG is relatively stable in 8 M urea or 4 M guanidine, but inactivated by performic acid oxidation or treatment with neuraminidase. Antiserum to PMSG was characterized by agar diffusion, immunoelectrophoresis, and quantitative precipitin reactions; it was specific for PMSG and did not cross react with human or ovine interstitial cell-stimulating hormone and follicle-stimulating hormone.
AB - Highly purified pregnant mare serum gonadotropin (PMSG) can be prepared from crude commercial preparations of PMSG by chromatography on sulfoethyl-Sephadex C-50 and gel filtration on Sephadex G-100. The preparation was examined by disc electrophoresis and gel filtration and found to be of high purity. Amino acid analysis shows similarities to pituitary gonadotropins. The PMSG contains a high content of proline and cystine and low amounts of the aromatic amino acids. Phenylalanine is the major amino terminal amino acid. The carbohydrate content totals 45% of which 10% is the content of sialic acid. The PMSG is relatively stable in 8 M urea or 4 M guanidine, but inactivated by performic acid oxidation or treatment with neuraminidase. Antiserum to PMSG was characterized by agar diffusion, immunoelectrophoresis, and quantitative precipitin reactions; it was specific for PMSG and did not cross react with human or ovine interstitial cell-stimulating hormone and follicle-stimulating hormone.
UR - http://www.scopus.com/inward/record.url?scp=0015507840&partnerID=8YFLogxK
U2 - 10.1016/0005-2795(72)90168-7
DO - 10.1016/0005-2795(72)90168-7
M3 - Article
C2 - 4622386
AN - SCOPUS:0015507840
SN - 0005-2795
VL - 263
SP - 139
EP - 148
JO - BBA - Protein Structure
JF - BBA - Protein Structure
IS - 1
ER -