Abstract
The molecular weight of Nephila clavata spider silk was determined to be ca. 600 kDa, under unreduced conditions, corresponding to its natural state, using the sodium dodecyl sulfate polyacrylamide gel electrophoresis method and a protein marker with a maximum molecular weight of 500 kDa. The addition of 2-mercaptoethanol into the spider silk solution decreased the molecular weight from ca. 600 kDa to ca. 270 kDa. Such a dramatic decrease in the molecular weight was ascribed to the presence of 2-mercaptoethanol as a reductant. This finding indicates the possibility that the reduction process cleaved the disulfide bonds formed between the spider silk proteins and then drastically decreased the molecular weight from ca. 600 to ca. 270 kDa. These results suggest that N. clavata spider silk proteins might consist of two proteins with a molecular weight of ca. 270 kDa that are crosslinked by disulfide bonds and exist as a dimer of ca. 600 kDa. Band patterns for N. clavata spider silk protein and for three different markers in 3% SDS-PAGE. M: marker, A: spider silk solution under a reduced state, B: spider silk solution under an unreduced state. The reduction due to a reductant cleaves the disulfide bonds and decreases the molecular weight from ca. 600 to ca. 270 kDa. Spider silk protein with ca. 600 kDa is suggested to be crosslinked by disulfide bonding between the two proteins.
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