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Acidic mammalian chitinase is a proteases-resistant glycosidase in mouse digestive system
TLDR
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.
Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs
TLDR
The data suggest that human AMCase has lost its chitinolytic activity by integration of nsSNPs during evolution and that the enzyme can be reactivated by introducing amino acids conserved in the mouse counterpart.
Chitin digestibility is dependent on feeding behaviors, which determine acidic chitinase mRNA levels in mammalian and poultry stomachs
TLDR
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.
Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry
TLDR
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.
Protein A-Mouse Acidic Mammalian Chitinase-V5-His Expressed in Periplasmic Space of Escherichia coli Possesses Chitinase Functions Comparable to CHO-Expressed Protein
TLDR
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.
Improved fluorescent labeling of chitin oligomers: Chitinolytic properties of acidic mammalian chitinase under somatic tissue pH conditions.
TLDR
An improved method for chitin oligosaccharides suppressing this side reaction by pre-acidification of the fluorophore-labeling reaction mixture is established and it is found that AMCase produced dimer of N-acetyl-d-glucosamine (GlcNAc) at strong acidic to neutral condition.
Functional Properties of the Catalytic Domain of Mouse Acidic Mammalian Chitinase Expressed in Escherichia coli
TLDR
Results indicate that the primary structure of CatD is sufficient to form a proper tertiary structure required for chitinolytic activity, recognize chitin substrates and degrade them in the absence of a CBD.
Functional Properties of Mouse Chitotriosidase Expressed in the Periplasmic Space of Escherichia coli
TLDR
It is indicated that Chit1 degrades chitin substrates under physiological conditions and suggest its important pathophysiological roles in vivo.
Protease resistance of porcine acidic mammalian chitinase under gastrointestinal conditions implies that chitin-containing organisms can be sustainable dietary resources
TLDR
It is reported that pig AMCase is stable in the presence of other digestive proteases and functions as chitinolytic enzyme under the gastrointestinal conditions and indicates that chitin-containing organisms may be a sustainable feed ingredient in pig diet.
Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH
TLDR
The results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs.
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