Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Metabolism of the Hemin Chromoproteins

Metabolism of the Hemin Chromoproteins REVIEWS SOCIETY PHYSIOLOGICAL OCTOBER the Chromoproteid 2* * L. DRABKIN From the Department Univmity Physiological Chemistry, the Graduate School Me&&e, Pennsylvania, Ph&ade&hia, Pennsylvania BEPORE CHLOROPHYLL HEMOGLOBIN WERE KNOWN, the green foliage the red blood were fundamentals human experience. For primitive people ‘green’ was the symbol food, ‘red’ vigor war. The instinctive appreciation was essentially sound, though the present-day specialist substitutes ‘photosynthesis’ for ‘food, ’ ‘energy exchange’ for ‘vigor.’ With bigger better instruments to aid our senses, details in abundance have been revealed with reference to the chemistry function the principal , hemoglobin, myoglobin, cytochrome c its oxidase catalase. The prosthe tic iron complex, present in the molecul .ar archi tecture these proteins, 1s a natural tag, responsible both for their attribute eliciting the sensation color for their T ONG L4 l Much the writer’s work on chromoprotein , cited in this review, was aided by generous financial support from the fice Naval Research was done under contract between that fice the University Pennsylvania. * , used in the generic sense, has connotations similar to that the term heme. It is an iron-containing metalloporphyrin. There are 4 synthetic etioporphyrin types or classes, which only I III are biological interest. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Physiological Reviews The American Physiological Society

Metabolism of the Hemin Chromoproteins

Physiological Reviews , Volume 31: 345 – Oct 1, 1951

Loading next page...
 
/lp/the-american-physiological-society/metabolism-of-the-hemin-chromoproteins-7QdN8i5LNm

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
The American Physiological Society
Copyright
Copyright © 1951 the American Physiological Society
ISSN
0031-9333
eISSN
1522-1210
Publisher site
See Article on Publisher Site

Abstract

REVIEWS SOCIETY PHYSIOLOGICAL OCTOBER the Chromoproteid 2* * L. DRABKIN From the Department Univmity Physiological Chemistry, the Graduate School Me&&e, Pennsylvania, Ph&ade&hia, Pennsylvania BEPORE CHLOROPHYLL HEMOGLOBIN WERE KNOWN, the green foliage the red blood were fundamentals human experience. For primitive people ‘green’ was the symbol food, ‘red’ vigor war. The instinctive appreciation was essentially sound, though the present-day specialist substitutes ‘photosynthesis’ for ‘food, ’ ‘energy exchange’ for ‘vigor.’ With bigger better instruments to aid our senses, details in abundance have been revealed with reference to the chemistry function the principal , hemoglobin, myoglobin, cytochrome c its oxidase catalase. The prosthe tic iron complex, present in the molecul .ar archi tecture these proteins, 1s a natural tag, responsible both for their attribute eliciting the sensation color for their T ONG L4 l Much the writer’s work on chromoprotein , cited in this review, was aided by generous financial support from the fice Naval Research was done under contract between that fice the University Pennsylvania. * , used in the generic sense, has connotations similar to that the term heme. It is an iron-containing metalloporphyrin. There are 4 synthetic etioporphyrin types or classes, which only I III are biological interest.

Journal

Physiological ReviewsThe American Physiological Society

Published: Oct 1, 1951

There are no references for this article.