1978
DOI: 10.1042/bj1730553
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Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH

Abstract: Maltase-glucoamylase, a microvillous membrane ectoenzyme, was solubilized from rat intestinal mucosa by digestion with papain and subsequently purified to homogeneity with an overall yield of 10–20%. An antibody to the purified enzyme formed a single precipitin line in immunodiffusion experiments with an intestinal homogenate. The enzyme was shown to be an acidic glycoprotein (20% sugar by weight) which contained low amounts of cysteine and no sialic acid. At pH3–6, maltase activity was slowly lost, but the en… Show more

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Cited by 61 publications
(41 citation statements)
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“…The specific activity obtained was smaller (20-35 Ujmg) than reported earlier for both papain and detergent-solubilized forms of rat maltase/glucoamylase [5,11], but of the same size as reported for papain-solubilized rabbit maltase/glucoamylase [7].…”
Section: Purification Of Maltase/glucoamylasecontrasting
confidence: 50%
See 1 more Smart Citation
“…The specific activity obtained was smaller (20-35 Ujmg) than reported earlier for both papain and detergent-solubilized forms of rat maltase/glucoamylase [5,11], but of the same size as reported for papain-solubilized rabbit maltase/glucoamylase [7].…”
Section: Purification Of Maltase/glucoamylasecontrasting
confidence: 50%
“…Rat intestinal maltase/glucoamylase in both papain-solubilized and Triton-solubilized forms has been reported to have a molecular weight of 500000 [5,11], with subunits having molecular weights of 245000 and 134000. Analytical ultracentrifugation studies [S, 301 performed on the papain-solubilized forms of human and rabbit maltase/glucoamylase have revealed molecular weights of 21 0000-200000, which fit our data on the papain maltase/glucoamylase.…”
Section: S T Y M C F L L Y Pmentioning
confidence: 99%
“…Unlike other amylases, it can catalyse the hydrolysis of the 1,6-a-glycosidic linkage. This enzyme complex has been purified to varying degrees from different animal species (Seetharam et al, 1970;Schlegal-Haueter et al, 1972;Kelly & Alpers, 1973) and to homogeneity from rat (Flanagan & Forstner, 1978) and rabbit * To whom reprint requests should be addressed. (Sivakami & Radhakrishnan, 1973).…”
mentioning
confidence: 99%
“…In addition to a major band of Mr 500000, which corresponds to the neutral maltase peak of 550000 observed on gel filtration, this procedure reveals a minor fraction of an Mr-260 000 active protein. This minor band may be attributed to a partial dissociation of a polymeric or aggregated protein under the electrophoresis conditions (Flanagan & Forstner, 1978;Sorensen et al, 1982;Lee & Forstner, 1984;Noren et al, 1986). Further studies on the quaternary structure of human granulocytic neutral maltase are in progress.…”
Section: Discussionmentioning
confidence: 99%