The Primary Structure of Soybean (Glycine max) Leghemoglobin c.

Publisher Website
Google Scholar
Abstract
The primary structure of soybean (G. max. cv. Fiskeby) leghemoglobin c was determined. The polypeptide chain consists of 143 amino acid residues and has a MW of 15,950. The sequence of leghemoglobin c completely differs at 6 positions from that of component a. Microheterogeneity was observed at 6 positions, one alternative always being identical with the corresponding amino acid residue in component a. Leghemoglobins c1 and c2 differ only at position 143, which is lysine in c1 and phenylalanine in c2. The discrepancies between the sequences of leghemoglobin c reported by Hurrell and Leach and by this report are discussed in detail.

This publication has 2 references indexed in Scilit: