TY - JOUR
T1 - Protein secretion in Tetrahymena thermophila. Characterization of the major proteinaceous secretory proteins
AU - Maihle, N. J.
AU - Satir, B. H.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1986
Y1 - 1986
N2 - The contents of mucocysts of the ciliated protozoan Tetrahymena thermophila comprise about 12 proteins, ranging in relative mobility (M(r)) from approximately 160,000 to 8,000. There are at least four families of sulfhydryl-linked mucocyst polypeptides. One of these families includes a prominent M(r) 34,000 protein, as determined by one- and two-dimensional gel electrophoresis. The M(r) 34,000 protein is resolved into two species in isoelectric focusing gels, with apparent pI values of 4.8 and 4.9; most of the other mucocyst proteins also exhibit acidic apparent isoelectric points. The identity of the major M(r) 34,000 protein as a bona fide mucocyst component is substantiated by indirect immunofluorescent localization of this protein in a linear punctate pattern coincident with the localization of mucocysts in these cells; this pattern of localization can be abolished by stimulation of synchronous secretion and is absent in a mutant strain devoid of these secretory organelles (Maihle, N.J., and Satir, B.H. (1985a) J. Cell Sci. 78, 49-65).
AB - The contents of mucocysts of the ciliated protozoan Tetrahymena thermophila comprise about 12 proteins, ranging in relative mobility (M(r)) from approximately 160,000 to 8,000. There are at least four families of sulfhydryl-linked mucocyst polypeptides. One of these families includes a prominent M(r) 34,000 protein, as determined by one- and two-dimensional gel electrophoresis. The M(r) 34,000 protein is resolved into two species in isoelectric focusing gels, with apparent pI values of 4.8 and 4.9; most of the other mucocyst proteins also exhibit acidic apparent isoelectric points. The identity of the major M(r) 34,000 protein as a bona fide mucocyst component is substantiated by indirect immunofluorescent localization of this protein in a linear punctate pattern coincident with the localization of mucocysts in these cells; this pattern of localization can be abolished by stimulation of synchronous secretion and is absent in a mutant strain devoid of these secretory organelles (Maihle, N.J., and Satir, B.H. (1985a) J. Cell Sci. 78, 49-65).
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M3 - Article
C2 - 3519610
AN - SCOPUS:0022859954
SN - 0021-9258
VL - 261
SP - 7566
EP - 7570
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 16
ER -