scispace - formally typeset
Journal ArticleDOI

Cleavage of the haem-protein link by acid methylethylketone

F.W.J. Teale
- 01 Jan 1959 - 
- Vol. 35, pp 543-543
Citations
More filters
Book ChapterDOI

Determination of carbonyl content in oxidatively modified proteins.

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
More filters
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.

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.
Related Papers (5)