The contractile proteins of the human myometrium.
The contractile proteins of the human myometrium were quantified and characterized in order to investigate their possible modifications during pregnancy. The myosin concentration was found to be 1 to 5 mg/g of tissue, while actin concentration ranged from 16 to 60 mg/g, leading to an actin/myosin ratio higher (Mean = 14) than in other smooth muscles. Purified myosin submitted to two-dimensional gel electrophoresis exhibited two isoelectric forms for the 17 KD Light Chain, the more acidic being predominant in the pregnant organ, the more basic in the non gravid one. The mobility of myosin of form filaments was studied using electron microscopy. Only the myosin purified from gravid uteri in its phosphorylated form did aggregate in long bipolar filaments. Actin was characterized in crude muscle extracts using two-dimensional gel electrophoresis. It appeared in three forms differing by their isoelectric points. The more basic form (gamma) predominates in the pregnant organ, as soon as 17 weeks of pregnancy, while in the non-pregnant uterus it is the intermediate (beta) form which is predominant.
D003285:Contractile Proteins / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D008854:Microscopy, Electron; D008970:Molecular Weight; D009215:Myometrium / Q000032:analysis*; D009218:Myosins / Q000032:analysis; D010766:Phosphorylation; D014590:Uterine Contraction
D003285:Contractile Proteins; D009218:Myosins