Intra-assay Precision (Precision within an assay): CV%<8%
Three samples of known concentration were tested twenty times on one plate to assess.
Inter-assay Precision (Precision between assays):CV%<10%
Three samples of known concentration were tested in twenty assays to assess.
線性度:
To assess the linearity of the assay, samples were spiked with high concentrations of human α-Glucosidase in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
Sample
Serum(n=4)
1:20
Average %
95
Range %
85-103
1:40
Average %
90
Range %
85-99
1:80
Average %
95
Range %
91-102
1:100
Average %
89
Range %
81-97
回收率:
The recovery of human α-Glucosidase spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
Sample Type
Average % Recovery
Range
Serum (n=5)
95
85-101
EDTA plasma (n=4)
93
87-99
標(biāo)準(zhǔn)曲線:
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing.
基因功能參考文獻(xiàn):
Mechanistic Pathway on Human alpha-Glucosidase Maltase-Glucoamylase Unveiled by QM/MM Calculations PMID: 29548257
MGAM, or nearby regulatory elements, may be involved in the etiology of oral clefts. PMID: 25776870
Starch internal structure modulates its susceptibility to MGAM. The internal branch amounts negatively affect the glucose release rate. PMID: 25037326
Findings suggest that C-terminal subunits of recombinant maltase-glucoamylase (MGAM) assists alpha-amylase in digesting starch molecules and potentially may compensate for developmental or pathological amylase deficiencies. PMID: 22563462
These results suggest that the N-terminal and C-terminal catalytic domains of maltase-glucoamylase differ in their substrate specificities and inhibitor tolerance despite their structural relationship PMID: 22036121
we report crystal structures of C-terminal maltase-glucoamylase alone at a resolution of 3.1 angstroms, and in complex with its inhibitor acarbose PMID: 22058037
analysis of substrate selectivity of human maltase-glucoamylase and sucrase-isomaltase N-terminal domains PMID: 20356844
genetic analysis of MGAM, exon boundaries, and chromosome mapping PMID: 12547908
Raw starch granule degradation with recombinanat human MGAM indicates that pancreatic alpha-amylase hydrolysis is not a requirement for native starch digestion in the human small intestine. PMID: 17485087
Intestinal maltase-glycoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. PMID: 18036614
Acarbose has been found to improve insulin levels and thus glucose/insulin ratios more effectively in overweight patients compared with nonoverweight patients with PCOS. PMID: 18377903
This study reported the first diagnosed Finnish patient with a phenotype compatible with the late-onset form of Pompe disease. Molecular genetic analysis of the GAA gene revealed a novel missense mutation (Y575X),combined with (P545L) mutation. PMID: 19472353
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亞細(xì)胞定位:
Apical cell membrane; Single-pass type II membrane protein. Note=Brush border.
蛋白家族:
Glycosyl hydrolase 31 family
組織特異性:
Expressed in small intestine, granulocyte, and kidney but not in salivary gland or pancreas.