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- W2025869635 abstract "Monkey placental lactogen (MPL), a protein which cross-reacts with antisera to human growth hormone (HGH) and human placental lactogen (HPL), has been purified from extracts of full-term rhesus monkey placentae by ammonium sulfate precipitation, gel filtration on Sephadex followed by ionexchange chromatography. Two electrophoretically distinct components were obtained in a total yield ranging from 10 to 15 mg/kg wet wt. The electrophoretic mobility of the major component MPL-2 in polyacrylamide gel at pH 8.3 was more anodal than MPL-1, HPL and HGH. The yield of MPL-1 was about half that of MPL-2. Both components appeared to have a molecular weight between 28,000 and 29,000 estimated by gel filtration on Sephadex G-100; however, electrophoresis in polyacrylamide gel containing dodecyl sulfate indicated lower values: 22,500 and 21,000 for MPL-1 and MPL-2, respectively. Amino acid compositions of MPL-1 and MPL-2 were determined and compared with those of HGH and HPL. Both components of MPL are very similar in amino acid composition to those of HPL and HGH. The major differences are in the contents of histidine, tyrosine and tryptophan. Comparison of peptides maps of a tryptic digest of MPL, HPL and HGH revealed some similarity in the peptide patterns. (Endocrinology89: 631, 1971)" @default.
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- W2025869635 date "1971-09-01" @default.
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- W2025869635 title "Purification and Characterization of Monkey Placental Lactogen" @default.
- W2025869635 doi "https://doi.org/10.1210/endo-89-3-631" @default.
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