منابع مشابه
Membranes of the Human Pepsinogen Granule
Robertson's comprehensive study of the ultrastructure of cell membranes and membranous cell organelles (Robertson, 1957) demonstrated that many cytoplasmic membranes have basically a similar appearance. The appearance of these membranes when cut in cross-section and seen in the electron microscope is two dark lines about 20 A thick, separated by a less dense space of about 35 A. Conceiving of t...
متن کاملRadioimmunoassay of human pepsinogen A and pepsinogen C.
We describe the development of radioimmunoassays to measure both human pepsinogen A and pepsinogen C concentrations in serum. The antibodies were raised in goats by immunization with purified pepsinogen A or C. The affinity constants of the respective antibodies were 20.10(10) l/mol and 7.10(10) l/mol. Pepsinogens A and C were labeled with Na 125I by the chloramine T method. The binding between...
متن کاملPrimary structure of human pepsinogen gene.
A recombinant clone, which covers the pepsinogen gene in a single insert, has been isolated by screening a library of human genomic DNA, using a swine pepsinogen cDNA as a probe. Sequence analysis of coding DNA segments of the clone revealed that the pepsinogen gene occupies approximately 9.4-kilobase pairs of the genomic DNA and is separated into nine exons by eight introns of various lengths....
متن کاملEvidence for tubulin-binding sites on cellular membranes: plasma membranes, mitochondrial membranes, and secretory granule membranes
We describe the interaction of pure brain tubulin with purified membranes specialized in different cell functions, i.e., plasma membranes and mitochondrial membranes from liver and secretory granule membranes from adrenal medulla. We studied the tubulin-binding activity of cellular membranes using a radiolabeled ligand-receptor assay and an antibody retention assay. The tubulin-membrane interac...
متن کاملInteraction of calmodulin with adrenal chromaffin granule membranes.
We have reported that calmodulin bound specifically to catecholamine-containing secretory granules of adrenal medullary chromaftin cells [I]. Binding was dependent upon pM levels of Ca2+ and saturated at a low level (3.3. pmol calmodulin/mg granule membrane protein). Additionally, we observed that the phosphorylation of membrane polypeptides of M, 59 000, 58 000 and 53 000 was stimulated by cal...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The Journal of Biophysical and Biochemical Cytology
سال: 1961
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.10.1.145