Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Ryu, K.-S.
Right arrow Articles by Kim, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ryu, K.-S.
Right arrow Articles by Kim, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1998, Vol. 123, No. 1 55-61
© 1998 Japanese Biochemical Society

research-article

Interaction of Glucagon with Dimyristoylphosphatidylcholine in Vesicular and Discoidal Complexes

Kyoung-Seok Ryu, Hyun-Sook Han1 and Hyoungman Kim2

Department of Biological Sciences, Korea Advanced Institute of Science and Technology 373-1, Kusong-dong, Yusong-gu, Taejon, 305-701, Korea

2To whom correspondence should be addressed. Tel: +81-82-042-869-4011, Fax: +81-82-042-869-2610, E-mail: hmkim.sorak. kaist.ac.kr

Glucagon fragments dimyristoylphosphatidylcholine liposomes into discoidal complex under appropriate conditions. The concentration of glucagon required to fragment the vesicles increases with increasing pH, which appears to be related to the glucagon binding. It was also observed that the fragmentation is facilitated by NaCl, which is also due to increased glucagon binding. From the quenching of Trp fluorescence by doxyl group located at various positions of the acyl chain of the lipid, Trp of glucagon was found to be located close to the bilayer surface in the vesicular complex. However, the Trp fluorescence was quenched by the doxyl group in the discoidal complex to an equal extent regardless of the position of this spin label in the acyl chain. This and the results of second derivative UV spectroscopy of Tyr suggested that segments including Tyr-13 and Trp-25 are involved in the discoidal complex formation and that the orientation of glucagon is not normal to the bilayer surface.

1Present address: Korea Research and Development Information Center, Yusong P.O. Box 122, Taejon, 305-701, Korea.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.