The enzymic activity of transient sodium dodecyl sulphate-protein complexes of rat intestinal maltase-glucoamylase formed during dissociation [proceedings]
- PMID: 21824
- DOI: 10.1042/bst0051542
The enzymic activity of transient sodium dodecyl sulphate-protein complexes of rat intestinal maltase-glucoamylase formed during dissociation [proceedings]
Similar articles
-
Enzyme activity in partly dissociated fragments of rat intestinal maltase/glucoamylase.Biochem J. 1979 Feb 1;177(2):487-92. doi: 10.1042/bj1770487. Biochem J. 1979. PMID: 35155 Free PMC article.
-
Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH.Biochem J. 1978 Aug 1;173(2):553-63. doi: 10.1042/bj1730553. Biochem J. 1978. PMID: 29602 Free PMC article.
-
A comparison of the active site of maltase-glucoamylase from the brush border of rabbit small intestine and kidney by chemical modification studies.Biochem J. 1991 Mar 1;274 ( Pt 2)(Pt 2):349-54. doi: 10.1042/bj2740349. Biochem J. 1991. PMID: 2006904 Free PMC article.
-
Ontogeny of enzymes in the small intestine.Annu Rev Physiol. 1985;47:231-45. doi: 10.1146/annurev.ph.47.030185.001311. Annu Rev Physiol. 1985. PMID: 3888075 Review. No abstract available.
-
Maltase Has Most Versatile α-Hydrolytic Activity Among the Mucosal α-Glucosidases of the Small Intestine.J Pediatr Gastroenterol Nutr. 2018 Jun;66 Suppl 3:S7-S10. doi: 10.1097/MPG.0000000000001954. J Pediatr Gastroenterol Nutr. 2018. PMID: 29762368 Review.
Cited by
-
Enzyme activity in partly dissociated fragments of rat intestinal maltase/glucoamylase.Biochem J. 1979 Feb 1;177(2):487-92. doi: 10.1042/bj1770487. Biochem J. 1979. PMID: 35155 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources