Abstract
Two methods were developed for the isolation of M r 30k kafirin protein from immature sorghum, one involving direct extraction with 20% (v/v) 2-mercaptoethanol (2-ME) and the other involving extraction with 20% (v/v) 2-ME followed by reversed-phase high performance liquid chromotography (RP-HPLC). The amino acid compositions of these isolated proteins were similar to each other and to a partially purified M r 30k kafirin from mature sorghum grain. These M r , 30k kafirins contained high levels of cysteine, proline and histidine, with low levels of aspartic acid and lysine. The molecular weight, solubility, and amino acid composition of M r 30k kafirin were similar to values published for maize gamma-zein. Structural similarity between gamma-zein and M r 30k kafirin was demonstrated through an immunological study showing cross-reactivity of the M r 30k kafirin protein and a gamma-zein antiserum. This high-cysteine M r 30k kafirin protein was named gamma-kafirin based on similarities in molecular weight, solubility and structure between it and gamma-zein of maize.
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