Pachytene spermatocytes isolated from immature rat testis were cultured for 6 h in the presence of [35S]methionine and the macromolecules present in the culture medium were analyzed by one-dimensional and two-dimensional gel electrophoresis. The electrophoretic profiles obtained showed a limited number of polypeptides, some of them consisting of families of spots with the same molecular weight but a different isoelectric point. The reproducibility of the results and the unaltered metabolic activity of the cells during culture time, indicate that the macromolecules present in the medium do not represent degradative products of the cells. Part of the detected macromolecules are considered secreted proteins since the addition of monensin to the cells induces their disappearance from the culture medium.
Evidence of protein secretion by cultured pachytene spermatocytes / M., Galdieri; Monaco, Lucia. - In: CELL DIFFERENTIATION. - ISSN 0045-6039. - STAMPA. - 13:1(1983), pp. 49-55.
Evidence of protein secretion by cultured pachytene spermatocytes.
MONACO, Lucia
1983
Abstract
Pachytene spermatocytes isolated from immature rat testis were cultured for 6 h in the presence of [35S]methionine and the macromolecules present in the culture medium were analyzed by one-dimensional and two-dimensional gel electrophoresis. The electrophoretic profiles obtained showed a limited number of polypeptides, some of them consisting of families of spots with the same molecular weight but a different isoelectric point. The reproducibility of the results and the unaltered metabolic activity of the cells during culture time, indicate that the macromolecules present in the medium do not represent degradative products of the cells. Part of the detected macromolecules are considered secreted proteins since the addition of monensin to the cells induces their disappearance from the culture medium.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.