Reduced level of secretion and absence of subunit combination for the fibroin synthesized by a mutant silkworm, Nd(2).
Fibroin
Chain (unit)
DOI:
10.1083/jcb.99.6.2005
Publication Date:
2004-05-14T23:04:59Z
AUTHORS (6)
ABSTRACT
Fibroin is normally composed of one H chain (350 kd) and L (25 which are connected by disulfide bond(s). However, the small amount fibroin secreted into lumen posterior silk gland Nd(2) (naked pupa) mutant does not contain chain, although mRNA present synthesized in cells mutant. In a hybrid silkworm, Nd(2)/Tamanashikasuri, where Tamanashikasuri normal producer fibroin, from two alleles distinguishable electrophoretically. It demonstrated using this system that allele can combine with H-L complex normally. another system, Nd(2)/J-131, J-131 derived due to different electrophoretic mobility chain. The while devoid its secretion greatly reduced. We evidence suggesting structurally abnormal discuss how subunit structure advantageous fibroin.
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