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Characterization of heme lipoprotein...

Cordill, William Justin.

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Characterization of heme lipoprotein in ixodid tick saliva and hemolymph.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Characterization of heme lipoprotein in ixodid tick saliva and hemolymph./
Author:	Cordill, William Justin.
Description:	103 p.
Notes:	Adviser: Jack W. Dillwith.
Contained By:	Masters Abstracts International46-01.
Subject:	Biology, Entomology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1445921
ISBN:	9780549126966

Characterization of heme lipoprotein in ixodid tick saliva and hemolymph.
Cordill, William Justin.

Characterization of heme lipoprotein in ixodid tick saliva and hemolymph. - 103 p.

Adviser: Jack W. Dillwith.

Thesis (M.S.)--Oklahoma State University, 2007.

Scope and method of study. This study characterized heme lipoprotein (HeLp), the most abundant protein in Ixodid tick hemolymph and saliva using a number of biochemical and molecular methods.

ISBN: 9780549126966Subjects--Topical Terms:

1018619
Biology, Entomology.

Characterization of heme lipoprotein in ixodid tick saliva and hemolymph.
LDR:01982nam 2200325 a 45 001 939020
005 20110512
008 110512s2007 eng d
020 $a 9780549126966
035 $a (UMI)AAI1445921
035 $a AAI1445921
040 $a UMI $c UMI
100 1 $a Cordill, William Justin. $3 1263003
245 1 0 $a Characterization of heme lipoprotein in ixodid tick saliva and hemolymph.
300 $a 103 p.
500 $a Adviser: Jack W. Dillwith.
500 $a Source: Masters Abstracts International, Volume: 46-01, page: 0255.
502 $a Thesis (M.S.)--Oklahoma State University, 2007.
520 $a Scope and method of study. This study characterized heme lipoprotein (HeLp), the most abundant protein in Ixodid tick hemolymph and saliva using a number of biochemical and molecular methods.
520 $a Findings and conclusions. This study revealed that HeLp is the most abundant protein in the hemolymph and saliva of all Ixodid ticks examined. Although highly conserved, the proteins are not identical among these species. HeLp is a heterodimer of homodimers, having the formula B2A2. The glycosylated HeLp-B subunit dimerizes with at least one intersubunit disulfide linkage. In both hemolymph and saliva, proteins appearing to be precursors occur in smaller titers. HeLp is translated as a single polypeptide precursor including a signal peptide, the HeLp-B sequence, a processing site, and HeLp-A sequence. The cDNA sequence reveals that HeLp is homologous to vitellogenin. A molecular model of HeLp-B was constructed; supporting our earlier studies and will be a useful tool for further studies.
590 $a School code: 0664.
650 4 $a Biology, Entomology. $3 1018619
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0307
690 $a 0353
690 $a 0487
710 2 0 $a Oklahoma State University. $b Entomology. $3 1263004
773 0 $t Masters Abstracts International $g 46-01.
790 $a 0664
790 1 0 $a Dillwith, Jack W., $e advisor
790 1 0 $a Jiang, Haobo $e committee member
790 1 0 $a Soulages, Jose $e committee member
791 $a M.S.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1445921