Structure and properties of hemocyanins. XVIII. Functional properties of chemically modified hemocyanin. Fixation of hemocyanin in the low and the high oxygen affinity state by reaction with a bifunctional imido ester
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00675a013
Reference16 articles.
1. Bates, R. C. (1954), Electrometric pH Determinations, New York, N.Y., Wiley, pp91 -125.
2. Molecular-Weight Analysis of Helix pomatia alpha-Hemocyanin in Guanidine Hydrochloride, Urea and Sodium Dodecylsulfate
3. Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric Proteins
4. Structure and function of hemocyanins VII. The smallest subunit of α- and β-hemocyanin of Helix pomatia: Size, composition, N- and C-terminal amino acids
5. Oxygen binding properties of haemocyanin from Levantina hierosolima
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1. Three-dimensional reconstruction of native Androctonus australis hemocyanin;Journal of Molecular Biology;1990-12
2. Electron microscopy of hemocyanins 1942–1986;Micron and Microscopica Acta;1986-01
3. Conformational Differences Between Oxy- and Deoxy-Hemocyanin;Invertebrate Oxygen Carriers;1986
4. An oxygenation-linked dye binding to Limulus polyphemus hemocyanin;European Journal of Biochemistry;1985-02
5. Binding of oxygen and carbon monoxide to arthropod hemocyanin: an allosteric analysis;Biochemistry;1985-01
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