Journal ArticleDOI
Cleavage of the haem-protein link by acid methylethylketone
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This article is published in Biochimica et Biophysica Acta.The article was published on 1959-01-01. It has received 1162 citations till now. The article focuses on the topics: Cleavage (embryo) & Hemeproteins.read more
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Book ChapterDOI
Determination of carbonyl content in oxidatively modified proteins.
Rodney L. Levine,Donita Garland,Cynthia N. Oliver,Adolfo Amici,Isabel Climent,Anke-G. Lenz,Bong-Whan Ahn,Shmuel Shaltiel,Earl R. Stadtman +8 more
TL;DR: This chapter discusses methods to determine carbonyl content in oxidatively modified proteins and quantitated protein-bound pyruvoyl groups through formation of a Schiff base with p-aminobenzoic acid followed by reduction with cyanoborohydride.
Journal ArticleDOI
Amyloid fibrils from muscle myoglobin
TL;DR: Even an ordinary globular protein can assume a rogue guise if conditions are right and the molecule can be tricked into thinking it is another protein.
Journal ArticleDOI
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
TL;DR: Hydrogen exchange pulse labeling and stopped-flow circular dichroism were used to establish that the structure of the earliest detectable intermediate formed during refolding of apomyoglobin corresponds closely to that of a previously characterized equilibrium molten globule.
Journal ArticleDOI
Structural characterization of a partly folded apomyoglobin intermediate.
TL;DR: A structural model is presented for the partly folded intermediate of native myoglobin in which a compact subdomain retains structure while the remainder of the protein is essentially unfolded.
Book ChapterDOI
Hemoglobin and myoglobin.
TL;DR: This chapter describes hemoglobin and myoglobin, and briefly describes some properties and reactions of their prosthetic group, mainly because the characteristic physiological functions of these proteins arise from the intrinsic reactivity of the heme.
References
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Journal ArticleDOI
Studies on the structure of hemoglobin I. Physicochemical properties of human globin
TL;DR: The most important physicochemical constants of human globin and its coupling capacity for hematin are reported.
Journal ArticleDOI
Protein coagulation and its reversal : the preparation of insoluble globin, soluble globin and heme.
M. L. Anson,Alfred E. Mirsky +1 more
TL;DR: The denatured globin may be largely converted into a soluble, apparently native form which can combine with heme to form hemoglobin, and the heme may be obtained in acetone-free, slightly alkaline solution without the use of strong alkali.
Journal ArticleDOI
Spectrophotometric studies iii. methemoglobin
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