Is the unique negatively charged polypeptide of crayfish yolk HDL a component of crustacean vitellin? Academic Article uri icon

abstract

  • The yolk protein of Cherax quadricarinatus contains six major high-density lipo- protein (HDL) subunits with the approximate molecular masses of 177, 155, 106, 95, 86, and 75 kDa, of which only the 106-kDa polypeptide is negatively charged. On the basis of their molecular weights, time of appearance and disappearance, their floating density and susceptibility to en- zyme degradation (by a serine proteinase), these six HDL polypeptides were classified into two subgroups. One group comprises the higher-molecular-weight compounds above 106 kDa, and the other includes the lower-molecular-weight compounds up to 95 kDa. Other than being different from the lower-molecular-weight polypeptides, the negatively charged 106-kDa polypeptide was significantly different from members of its higher-molecular-weight group belonging to a different, less abundant, yolk protein as shown by HPLC separation. Immunological studies and peptide mapping in which the 106-kDa polypeptide did not show similarity to any of the other HDL com- ponents confirmed these differences. Moreover, the amino acid composition of the 106-kDa polypep- tide was different from that of known vitellin from other crustacean species. This unique negatively charged polypeptide presents an enigma as it is known to be a secondary vitellogenic-related HDL polypeptide, immunolocalized in yolk globules; however, it is different to all the other HDL polypep- tides, thus presenting the question whether it is indeed a component of "classical" crustacean vitellin. J. Exp. Zool. 290:218-226, 2001. © 2001 Wiley-Liss, Inc.

publication date

  • January 1, 2001