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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.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Characterization of heme lipoprotein in ixodid tick saliva and hemolymph./
作者:
Cordill, William Justin.
面頁冊數:
103 p.
附註:
Adviser: Jack W. Dillwith.
Contained By:
Masters Abstracts International46-01.
標題:
Biology, Entomology. -
電子資源:
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.
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Characterization of heme lipoprotein in ixodid tick saliva and hemolymph.
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103 p.
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Adviser: Jack W. Dillwith.
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Source: Masters Abstracts International, Volume: 46-01, page: 0255.
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Thesis (M.S.)--Oklahoma State University, 2007.
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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
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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.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1445921
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