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University of Illinois at Urbana-Champaign
Characterization of the primary structure of a size-variant antifreeze peptide and the organization and structure of antifreeze peptide genes from the Antarctic eel pout Rhigophila dearborni
Abstract
dc:descriptionThe antarctic eel pout Rhigophila dearborni synthesizes three major antifreeze peptides (AFPs) which have been designated RD1, RD2 and RD3, and at least four minor ones. RD1 and RD2 both are 64 residues with a molecular weight (M.W.) of about 7000 Daltons. RD3 however appears to be twice as large with a M.W. of 14,000 Daltons. The primary structure of the size-variant RD3 was determined. The complete peptide sequence of RD3 was found to consist of two peptide sequences very similar to those of RD1 and RD2 joined head-to-tail by a 9-amino-acid connecting sequence that is not present in any characterized eel pout AFPs.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Physiology
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2011
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Wang, Xin
- Contributors dc:contributor
-
- DeVries, Arthur L.
Subjects
dc:subject × 3Rights
dc:rights- Statement dc:rights
-
- Copyright 1993 Wang, Xin
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
-
AAI9411815
(UMI)AAI9411815 - OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/18947