Abstract
The human interleukin-3 amino acid sequence contains two consensus sequences at Glu 22-His 26 and His 95-His 98 which are characteristic for zinc binding proteins. 252Cf plasma desorption mass spectrometry and Western blotting in combination with protease treatment have been used to localize the zinc binding site of human interleukin-3. Zinc binding, specific to protein and metal ion was determined by established protein chemistry methods. The affinity for zinc appeared to be significantly enhanced in the endo Lys-C fragments of amino acids (11–28) and (80–100) when the disulfide bridge between them was still intact. After treatment with endo Glu-C no zinc binding activity was observed. It can be concluded that the zinc binding in human interleukin-3 is largely determined by the presence of both parts of the interleukin-3 sequence which contain the theoretically predicted consensus sequence.
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