Add time:09/24/2019         Source:sciencedirect.com

Plasma from the Antarctic toothfish, Dissostichus mawsoni, a member of the advanced teleost Nototheniidae family, was analysed. Agarose gel electrophoresis showed a major diffuse anionic protein that bound [14C]palmitic acid but not 63Ni2+, and two more cationic proteins that bound 63Ni2+ but not palmitate. Oil Red O staining following cellulose acetate electrophoresis indicated that the palmitate binding protein was a lipoprotein. Two-dimensional electrophoresis showed that this palmitate binding band was composed of three proteins with Mr of 11, 30, and 42 kDa, without any trace of material at ∼65 kDa, the mass of albumin. N-terminal sequencing of the palmitate binding band gave a major sequence of DAAQPSQELR-, indicating a high degree of homology to apolipoprotein A-I (apo-AI), the major apolipoprotein of high density lipoprotein (HDL). N-terminal sequencing of the major nickel binding band produced a sequence with no homology to albumin. When ultracentrifugation was used to isolate the lipoproteins from Antarctic toothfish plasma, the palmitate binding protein was found solely in the lipoprotein fraction. In competitive binding experiments, added human albumin did not prevent palmitate binding to toothfish HDL. In conclusion, there is no evidence for albumin in Antarctic toothfish plasma and HDL assumes the role of fatty acid transport.

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