English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The blood of the Electric Ray contains a number of hemoglobin components. The primary structures of the alpha- and beta-chains of the main components are presented. These chains were purified by high-performance liquid chromatography, using a new buffer system. The alpha-chains consist of 141 residues, and the beta-chains of 142 residues; both are unblocked. The phylogenetic distances from human alpha- and beta-chains are 55% and 64% amino-acid exchanges, respectively. The relationship between primary structure and the lack of both a Bohr effect and any effector affinity is discussed, and interpreted on a molecular level with reference to the sequence presented. For the Bohr effect, the mutation beta 89 Asp----Lys is significant, while the mutations beta 2 His----Ser, beta 82 Lys----Asn and beta 142 His----Cys are important for the lack of effector affinity.

The Primary Structure of Electric Ray Hemoglobin (Torpedo marmorata). Bohr Effect and Phosphate Interaction