Abstract
Tarantula (Eurypelma californicum) hemocyanin (Hc) is a 1.7×106 molecular weight protein containing 24 subunits. These are not identical but belong to 7 different types, designated a-g. The quaternary structure of Eurypelma Hc has been revealed several years ago (1). This hemocyanin shows extremely strong positive cooperativity with nH values running up to 10. However, direct evidence for conformational changes upon oxygenation and deoxygenation of arthropod Hc has not yet been published to our knowledge. In the present paper we report fluorescence spectroscopic studies to detect such changes. The strong intrinsic tryptophan fluorescence cannot be used for this purpose, for it is nearly totally quenched upon oxygenation (2). Therefore we applied various extrinsic probes.
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