Journal
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
Volume 128, Issue 2, Pages 265-273Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S1096-4959(00)00323-7
Keywords
antifreeze glycoproteins; AFGP; molecular weight; teleost fish; thermal hysteresis; Gadus ogac; liposomes; phase transition; hypothermic protection; phospholipid membrane
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Antifreeze glycoproteins (AFGP) were isolated and purified from the blood plasma of rock cod (Gadus ogac), using DEAE-Bio-gel ion exchange chromatography, followed by high performance liquid chromatography (HPLC). The purified proteins were analyzed using polyacrylamide gel electrophoresis (PAGE), and electrospray mass spectrometry. The results indicated that rock cod synthesize seven size classes of glycoproteins, ranging from 2.6 to 24 kDa, with each size class containing multiple isoforms, Antifreeze activity, as determined by thermal hysteresis, indicated that the AFGP could be separated into two groups, with the larger size classes (molecular mass > 13 kDa) having approximately 3-4 times the activity of the smaller, proline containing, size classes (molecular mass < 10 kDa). All of the AFGP size classes prevented leakage From dielaidoylphosphatidylcholine (DEPC) liposomes as they were cooled through their phase transition temperature, with the larger size classes being approximately 4 times as effective as the smaller ones. It is hypothesized that AFGP prevent liposomes from leaking as they pass through the phase transition temperature by binding to the phospholipid membrane. (C) 2001 Elsevier Science Inc. All rights reserved.
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