Effect of W62G mutation of hen lysozyme on the folding in vivo.
In previous paper, we showed that W62G mutation caused ill effects at the early stages of folding of the reduced hen lysozyme in vitro. Here, we investigated whether the single mutation brings about drastic turn to in vivo folding of lysozyme. W62G lysozyme was secreted from yeast cells and then purified with ion-exchange chromatography. From the results of gel chromatography and peptide analysis, the species with two cysteines, Cys80 and Cys94, and non-native cystine, Cys64-Cys76, was partially present in secreted product of yeast containing gene for W62G lysozyme. Thus, it was suggested that W62G mutation also affected the in vivo folding of lysozyme.
Ohkuri
Takatoshi
T
Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan.
Imoto
Taiji
T
Ueda
Tadashi
T
D019943:Amino Acid Substitution; D000596:Amino Acids / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D009113:Muramidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D011485:Protein Binding; D017510:Protein Folding; D013329:Structure-Activity Relationship
D000596:Amino Acids; C421864:hen egg lysozyme; D009113:Muramidase