Changes in the protein conformation of human spermatozoal membranes after treatment with cyclic adenosine 3':5'-monophosphate and human follicular fluid.
Infrared spectra in the amide I and amide II regions of acrosomal membranes isolated from ejaculated human spermatozoa indicate the presence of a high proportion of the constitutive proteins in the most stable protein configuration, the antiparallel beta-conformation. Since the infrared spectra obtained with the membranes suspended in D2O or after extraction of the lipid components do not show any significant change, it can be postulated that the antiparallel pleated sheet conformation of human spermatozoal membrane proteins is independent of the hydrated state and of the lipid constitution of the membrane.
D000177:Acrosome / Q000187:drug effects* / Q000648:ultrastructure; D001826:Body Fluids / Q000502:physiology*; D002462:Cell Membrane / Q000187:drug effects / Q000648:ultrastructure; D000242:Cyclic AMP / Q000494:pharmacology*; D005260:Female; D006801:Humans; D008297:Male; D006080:Ovarian Follicle / Q000502:physiology*; D011487:Protein Conformation / Q000187:drug effects; D013075:Sperm Capacitation / Q000187:drug effects; D013094:Spermatozoa / Q000187:drug effects*
D000242:Cyclic AMP