id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-306067-ldn17pj8	Inoue, Satoshi	Assembly of the silk fibroin elementary unit in endoplasmic reticulum and a role of L‐chain for protection of α1,2‐mannose residues in N‐linked oligosaccharide chains of fibrohexamerin/P25	2003-12-19		.txt	text/plain	6302	274	61	These results suggest that the 30-kDa component is the ER form of fhx/P25 and the 27-kDa component represents fhx/P25 whose N-linked oligosaccharide chains lost their terminal a1,2-mannose residues by digestion with a1,2-manosidases in Golgi complex, and further imply that fhx/P25 in the elementary unit of the normal-level fibroin-producing breeds is largely resistant to the action of a1,2-mannosidases in Golgi complex and secreted as the ER-type 30-kDa form. It is thus conceivable that in the Nd-s D mutant silkworm, fhx/P25 in the L-chain-free H 6 fhx 1 -type elementary unit (Table 2) is processed efficiently by the action of Golgi a1,2-mannosidases to yield only the 27-kDa molecule in the secreted fibroin. In order to examine a role of L-chain in the protection of a1,2-mannose residues of fhx/P25 in the elementary unit, the Nd-s D mutant silkworm was subjected to transgenesis with the normal L-chain promoter/cDNA sequence together with a marker gene of DsRed2 (Fig. 4A) , and two transgenic lines L6 · 7 and L7-4 were selected.	./cache/cord-306067-ldn17pj8.txt	./txt/cord-306067-ldn17pj8.txt