Structural determination of an N-glycan moiety attached to the prothoracicotropic hormone from the silkmoth Bombyx mori-Reference-Cited by-同舟云学术

Structural determination of an N-glycan moiety attached to the prothoracicotropic hormone from the silkmoth Bombyx mori

Published:2014-08-03 Issue:8 Volume:78 Page:1381-1383
ISSN:0916-8451
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Nagata Shinji¹²,Kobayashi Jun³⁴,Kataoka Hiroshi¹²,Suzuki Akinori¹

Affiliation:

1. Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan

2. Department of Integrated Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan

3. Faculty of Engineering, Mie University, Tsu, Japan

4. Faculty of Agriculture, Department of Biological and Environmental Sciences, Yamaguchi University, Yamaguchi, Japan

Abstract

Abstract The predominant structure of the N-glycan on the prothoracicotropic hormone (PTTH) isolated from 1.8 million adult heads of silkmoths was determined to be Manα1-6Manβ1-4GlcNAcβ1-4(Fucα1-6)GlcNAc-OH, which is identical to that of the baculovirus-expressed recombinant PTTH. An ecdysis progression assay demonstrated that N-glycosylated PTTH exhibited a slightly higher activity than the recombinant PTTH without N-glycosylation produced by an Escherichia coli expression system.

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/article-pdf/78/8/1381/36801200/bbb1381.pdf

Reference16 articles.

1. Prothoracicotropic Hormone

2. Silk Moth Neuropeptide Hormones: Prothoracicotropic Hormone and Others

3. Control and Biochemical Nature of the Ecdysteroidogenic Pathway

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