Antifreeze Protein from Japanese Fish

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Type II antifreeze protein from a mid-latitude freshwater fish, Japanese smelt (Hypomesus nipponensis).

A lot of reports of antifreeze protein (AFP) from fish have been published, but no report has mentioned of commercialized mid-latitude fresh water fish which producing AFP in its body fluid. We found that the AFP in the body fluid of Japanese smelt (Hypomesus nipponensis) from mid-latitude fresh water was purified and characterized. The N-terminal amino acid sequence of the Japanese smelt AFP w...

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Antifreeze glycoproteins from Arctic fish.

Four species of fish in the Barents Sea of the Arctic, north of Norway and Russia, were caught and examined for the presence of antifreeze proteins in their blood sera. Only one species of Arctic fish, the polar cod (Boreogadus saida), was found to contain an antifreeze protein. Antifreeze glycoproteins were isolated and characterized from the blood serum of the Arctic fish, and their structure...

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Antifreeze Glycoprotein from an Antarctic Fish

Structural requirements for antifreeze and antilectin activities of the antifreeze glycoproteins from the Antarctic fish Trematomus borckgrevinki have been compared. Graded removal of different amounts of the disaccharide side chain by p elimination caused similar reductions in the capacities for depressing the freezing temperature of water (antifreeze activity) and for inhibiting hemagglutinat...

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Antifreeze Glycoproteins from an Antarctic Fish

A quasi-elastic light-scattering technique was used to study the hydrodynamic conformations of antifreeze glycoproteins from an Antarctic fish. Antifreeze glycoprotein is composed of repeating units of Ala-Ala-Thr, with each threonine O-linked to a disaccharide, and it exists as several polymers of different numbers of this repeating unit. Molecular weights of the two major active polymers are ...

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Antifreeze Protein Dimer

A naturally occurring tandem duplication of the 7-kDa type III antifreeze protein from Antarctic eel pout (Lycodichthys dearborni) is twice as active as the monomer in depressing the freezing point of a solution. We have investigated the basis for this enhanced activity by producing recombinant analogues of the linked dimer that assess the effects of protein size and the number and area of the ...

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ژورنال

عنوان ژورنال: Kobunshi

سال: 2006

ISSN: 0454-1138,2185-9825

DOI: 10.1295/kobunshi.55.494