Characterization and partial purification of a ganglioside-associated mitogen

Morgan, JI; Price, J; Seifert, W

doi:10.1111/j.1471-4159.1983.tb09046.x

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Characterization and partial purification of a ganglioside-associated mitogen

MPS-Authors

/persons/resource/persons289654

Morgan, JI
Seifert Group, Friedrich Miescher Laboratory, Max Planck Society;

/persons/resource/persons15822

Seifert, W
Seifert Group, Friedrich Miescher Laboratory, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Morgan, J., Price, J., & Seifert, W. (1983). Characterization and partial purification of a ganglioside-associated mitogen. Journal of Neurochemistry, 41(4), 1022-1029. doi:10.1111/j.1471-4159.1983.tb09046.x.

Cite as: https://hdl.handle.net/21.11116/0000-000D-2E87-8

Abstract

A nonganglioside factor(s) present in Sigma types II and III mixed bovine brain ganglioside preparations synergises with suboptimal amounts of serum to induce proliferation specifically in nondividing B 103 neuroblastoma cultures. The active substance is nondialysable and soluble in water as well as in chloroform-methanol mixtures of 1:1-4:1 (vol/vol). It is completely insoluble in ether and acetone at room temperature. Biological activity survives heating to 70 degrees C in the presence of 0.1 M HCl for 1 h as well as boiling at neutral pH. Loss of activity occurs on heating to 70 degrees C for 1 h with 1 M HCl or 1 M NaOH. The activity is insensitive to digestion with neuraminidase, trypsin, pronase, and phospholipases A2 and C. The factor cochromatographs with gangliosides on Dowex AG 50W and Sephadex G100 and is partially recovered with GM1 on DEAE-Sepharose, but may be isolated in a ganglioside-free fraction by sequential chromatography on Sephadex LH20 and silicic acid columns. The substance(s) has the properties of a water-soluble proteolipid protein, the amino acid composition being reported. It is not immunologically cross-reactive with antibodies to GM1 ganglioside or the major proteolipid protein of myelin.