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- W2016128340 abstract "Abstract 1. 1. Hyboscolex longiseta has a typical Annelid extracellular haemoglobin present in blood lacunae surrounding the gut, but no external gills. In EDTA-containing buffers this vascular haemoglobin dissociates into 133,000–139,000 components which correspond to 1/24th's of the original high mol. wt haemoglobin and which dissociate further when treated with 2-mercaptoethanol. 2. 2. Hyboscolex longiseta has a minor dimeric “myoglobin” and a major tetrameric “myoglobin”, the letter being identical to the haemoglobin contained in coelomic erythrocytes. There is also in muscle extracts a trace of what may be the original basic true myoglobin. 3. 3. Haemoglobin in muscle extracts has a low oxygen affinity, whereas haemoglobin in the vascular system has a high oxygen affinity. Thus, H. longiseta has evolved a reverse oxygen transfer system by a combination of increasing the oxygen affinity of the vascular haemoglobin and by changing the site of tissue expression of the erythrocyte haemoglobin so that much more of that protein is actually made in the body wall musculature as a “myoglobin”. 4. 4. High oxygen affinity respiratory proteins surrounding the gut are postulated to function in keeping low oxygen partial pressures. In this way polychaetes (which are part of the decomposer food chain) utilise detritus and associated microorganisms. Bacteria produce alcohols and other compounds, both from aerobic breakdown of lignins and other recalcitrant molecules and from anaerobic metabolism." @default.
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- W2016128340 title "Unusual pattern of haemoglobin tissue specificity in the “red maggot” worm Hyboscolex longiseta (polychaeta, scalibregmidae)" @default.
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- W2016128340 doi "https://doi.org/10.1016/0305-0491(88)90158-7" @default.
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