Powered by OpenAIRE graph
Found an issue? Give us feedback
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Comparative Biochemi...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Comparative Biochemistry and Physiology Part A Physiology
Article . 1975 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
versions View all 2 versions
addClaim

This Research product is the result of merged Research products in OpenAIRE.

You have already added 0 works in your ORCID record related to the merged Research product.

A hemeprotein implicated in oxygen transport into the eye of fish

Authors: Jonathan B. Wittenberg; Jonathan B. Wittenberg; Beatrice A. Wittenberg; Beatrice A. Wittenberg;

A hemeprotein implicated in oxygen transport into the eye of fish

Abstract

Abstract 1. 1. Following occlusion of the circulation to the eye of bluefish a ferric hemeprotein (or proteins) appears in the blood plasma of the ophthalmic blood vessels. 2. 2. This protein may play a role in the establishment of elevated oxygen pressures by the choroid rete mirabile. 3. 3. A hemeprotein (or proteins) is occasionally found in the systemic blood plasma of Amia calva. It combines reversibly with oxygen and with carbon monoxide. Ligand binding is co-operative, suggesting that the protein has two or more interacting subunits. 4. 4. Ferrous bluefish and Amia hemeproteins exhibit hemochromogen spectra, indicating that the distal ligand position of the heme is occupied by a nitrogenous (or sulfurous) ligand.

Related Organizations
Keywords

Hemeproteins, Carbon Monoxide, Chemical Phenomena, Pyridines, Fishes, Biological Transport, Eye, Oxygen, Chemistry, Species Specificity, Spectrophotometry, Animals, Oxidation-Reduction

  • BIP!
    Impact byBIP!
    citations
    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    6
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Average
    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    Top 10%
    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
    Average
Powered by OpenAIRE graph
Found an issue? Give us feedback
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
6
Average
Top 10%
Average
Upload OA version
Are you the author? Do you have the OA version of this publication?