Glycosylation events in the processing and secretion of pro-ACTH-endorphin in mouse pituitary tumor cells.
Glycosylation events in the processing and secretion of pro-ACTH-endorphin in mouse pituitary tumor cells.
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小鼠垂体肿瘤细胞中促肾上腺皮质激素原内啡肽加工和分泌中的糖基化事件。
DOI:
10.1021/bi00509a040
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Herbert,E
中科院分区:
文献类型:
--
作者:
Phillips,MA;Budarf,ML;Herbert,E
Marjorie A. Phillips,* Marcia L. Budarf, § and Edward Herbert* abstract: The glycosylation of pro-ACTH-endorphin and of its cleavage products has been studied in a mouse pituitary tumor cell line (AtT-20/D16v) by pulse labeling with^-la-beled sugars and amino acids followed by immunoprecipitation and sodium dodecyl sulfate slab gel electrophoresis. The results of this analysis indicate that there are two major intracellular species of pro-ACTH-endorphin (29K and 32K) and two minor species (30K and 34K). All of these species label with [3H] mannose,[3H] glucosamine, and [3H] galactose. In ad-dition, the 30K and 34K species label with [3H] fucose and are the major secreted forms of pro-ACTH-endorphin. Only the 29K and 32K forms are labeled after a short pulse with [35S] methionine. The 30K and 34K forms become labeled during a subsequent chase. Glycosidase digestion of Pronase glycopeptides derived from pro-ACTH-endorphin shows that the 29K and 32K forms contain high mannose type oligo-saccharides. The30K and 34K forms contain complex oli-gosaccharides with both core and branch sugars. These results
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DOI:
10.1016/s0021-9258(17)38161-9
发表时间:
1978-02
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
I. Tabas;S. Schlesinger;S. Kornfeld
通讯作者:
I. Tabas;S. Schlesinger;S. Kornfeld
影响因子:
4.8
作者:
R. Mains;B. Eipper
通讯作者:
B. Eipper
DOI:
10.1073/pnas.74.11.4826
发表时间:
1977
影响因子:
11.1
作者:
James L. Roberts;Edward Herbert
通讯作者:
Edward Herbert
影响因子:
4.4
作者:
S. Kessler
通讯作者:
S. Kessler
DOI:
10.1016/s0021-9258(17)33364-1
发表时间:
1976
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
B. Eipper;R. Mains;D. Guenzi
通讯作者:
D. Guenzi