Purification and composition of protein antifreezes with high cysteine contents from larvae of the beetle, Tenebrio molitor

Jean L. Patterson; John G. Duman

doi:10.1002/jez.1402190314

Purification and composition of protein antifreezes with high cysteine contents from larvae of the beetle, Tenebrio molitor

Jean L. Patterson, John G. Duman

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26 Scopus citations

Abstract

Two antifreeze proteins with thermal hysteresis activity (they depress the freezing point of aqueous solutions by a noncolligative mechanism well below the melting point) were purified from cold‐acclimated larvae of the beetle, Tenebrio molitor. Both proteins have unusual amino acid compositions consisting of high levels of cysteine (15.4 and 28.0 mol%).

Original language	English (US)
Pages (from-to)	381-384
Number of pages	4
Journal	Journal of Experimental Zoology
Volume	219
Issue number	3
DOIs	https://doi.org/10.1002/jez.1402190314
State	Published - 1982
Externally published	Yes

ASJC Scopus subject areas

Animal Science and Zoology

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10.1002/jez.1402190314

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title = "Purification and composition of protein antifreezes with high cysteine contents from larvae of the beetle, Tenebrio molitor",

abstract = "Two antifreeze proteins with thermal hysteresis activity (they depress the freezing point of aqueous solutions by a noncolligative mechanism well below the melting point) were purified from cold‐acclimated larvae of the beetle, Tenebrio molitor. Both proteins have unusual amino acid compositions consisting of high levels of cysteine (15.4 and 28.0 mol%).",

author = "Patterson, {Jean L.} and Duman, {John G.}",

year = "1982",

doi = "10.1002/jez.1402190314",

language = "English (US)",

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pages = "381--384",

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AU - Patterson, Jean L.

AU - Duman, John G.

PY - 1982

Y1 - 1982

N2 - Two antifreeze proteins with thermal hysteresis activity (they depress the freezing point of aqueous solutions by a noncolligative mechanism well below the melting point) were purified from cold‐acclimated larvae of the beetle, Tenebrio molitor. Both proteins have unusual amino acid compositions consisting of high levels of cysteine (15.4 and 28.0 mol%).

AB - Two antifreeze proteins with thermal hysteresis activity (they depress the freezing point of aqueous solutions by a noncolligative mechanism well below the melting point) were purified from cold‐acclimated larvae of the beetle, Tenebrio molitor. Both proteins have unusual amino acid compositions consisting of high levels of cysteine (15.4 and 28.0 mol%).

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Purification and composition of protein antifreezes with high cysteine contents from larvae of the beetle, Tenebrio molitor

Abstract

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