scispace - formally typeset
M

Masayoshi Sakaguchi

Researcher at Kogakuin University

Publications -  38
Citations -  692

Masayoshi Sakaguchi is an academic researcher from Kogakuin University. The author has contributed to research in topics: Chitinase & Chitin. The author has an hindex of 14, co-authored 38 publications receiving 545 citations.

Papers
More filters
Journal ArticleDOI

Acidic mammalian chitinase is a proteases-resistant glycosidase in mouse digestive system

TL;DR: Evidence is provided that acidic mammalian chitinase (AMCase) can function as a protease-resistant major glycosidase under the conditions of stomach and intestine and degrade chit in substrates to produce (GlcNAc)2, a source of carbon, nitrogen and energy.
Journal ArticleDOI

Chitin digestibility is dependent on feeding behaviors, which determine acidic chitinase mRNA levels in mammalian and poultry stomachs.

TL;DR: The results indicate that feeding behavior affects Chia expression levels as well as chitinolytic activity of the enzyme, and determines chitin digestibility in the particular animals.
Journal ArticleDOI

Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry

TL;DR: Functional similarity of chicken Chia with the mouse enzyme suggests that chitin-containing organisms can be used for alternative poultry diets not only as whole edible resources but also as enhancers of their nutritional value.
Journal ArticleDOI

Quantification of Chitinase mRNA Levels in Human and Mouse Tissues by Real-Time PCR: Species-Specific Expression of Acidic Mammalian Chitinase in Stomach Tissues.

TL;DR: A quantitative PCR system was developed to compare the mRNA levels between human and mouse tissues using a human-mouse hybrid standard DNA and showed that Chit1 mRNA is expressed at similar levels in normal human andmouse lung, whereas AMCase mRNA was not overexpressed innormal human stomach tissues.
Journal ArticleDOI

Protein A-mouse acidic mammalian chitinase-V5-His expressed in periplasmic space of Escherichia coli possesses chitinase functions comparable to CHO-expressed protein.

TL;DR: The E. coli-expressed Protein A-mouse AMCase-V5-His fusion protein possesses chitinase functions comparable to the CHO-expressive AMCase and can be used to elucidate detailed biomedical functions of the mouse AMCase.