Further characterization of the porcine LH subunits precursors in the translation products of pituitary RNAs.
We have shown that the precursors of porcine LH alpha and beta subunits have similar apparent molecular weights (Biochem. Biophys. Res. Comm., 1984, 118, 254). The aim of the present study was to characterize physiochemical features which permit to distinguish these precursors from each other. We report here that these precursors can be clearly distinguished by both their tryptic digests analyzed by one-dimension electrophoresis and their behavior in two-dimension electrophoresis whose first dimension was made in a non equilibrium pH gradient (2D-NEPHGE). The 2D-NEPHGE method developed in this study appears also useful to estimate simultaneously the translation activities of pituitary hormone mRNAs without a previous immunoprecipitation.
D000818:Animals; D002369:Castration; D004591:Electrophoresis, Polyacrylamide Gel; D015292:Glycoprotein Hormones, alpha Subunit; D007986:Luteinizing Hormone / Q000235:genetics* / Q000302:isolation & purification; D008297:Male; D010446:Peptide Fragments / Q000032:analysis / Q000235:genetics* / Q000302:isolation & purification; D010903:Pituitary Gland, Anterior / Q000378:metabolism*; D010908:Pituitary Hormones, Anterior / Q000235:genetics* / Q000302:isolation & purification; D010944:Plants / Q000378:metabolism; D011061:Poly A / Q000235:genetics; D014176:Protein Biosynthesis; D012313:RNA / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics*; D013552:Swine; D014908:Triticum / Q000378:metabolism
D015292:Glycoprotein Hormones, alpha Subunit; D010446:Peptide Fragments; D010908:Pituitary Hormones, Anterior; D012333:RNA, Messenger; D011061:Poly A; D012313:RNA; D007986:Luteinizing Hormone