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Abstract
The tissue distribution of the predominant hemolymph protein found throughout tick
development was examined in the hard tick, Dermacentor variabilis, and in the soft
tick, Ornithodoros parkeri. In D. variabilis, the predominant (purified) hemolymph
protein was a lipoglycoheme-carrier protein (DvCP) with a molecular weight of 200K.
A protein with a similar mobility on native-PAGE was found in fat body, salivary gland,
muscle and ovary from partially fed females which was most abundant in the plasma
and salivary gland. DvCP from plasma, salivary gland and fat body of partially fed
females consisted of two subunits on SDS-PAGE (98 and 92K). In replete females, only
salivary gland exhibited protein subunits equivalent to hemolymph CP. CP in salivary
gland and fat body stained positive for lipids. The concentration of CP in tissues
varied between partially fed and replete females, indicating a difference in the expression
and/or sequestration of CP during adult development. The predominant hemolymph carrier
protein from O. parkeri (OpCP) was purified to homogeneity for the first time and
is presumed to have similar functions to CP from D. variabilis. Purified OpCP exhibited
a molecular weight of 668K by native-PAGE. Unlike CP from D. variabilis, OpCP was
not detected in fat body or salivary gland tissues but occurred abundantly in coxal
fluid. By SDS-PAGE, purified hemolymph OpCP consisted of two major subunits (114 and
93K) and a less abundant protein with an apparent molecular weight of 48K. Purified
native OpCP was a lipoprotein like DvCP. A spectral analysis of purified OpCP failed
to demonstrate the presence of heme like that found for CP from D. variabilis, purified
by the same methods. However, plasma from O. parkeri contained heme with a lambda(max)
of 410nm.