The diversity of alkaline phosphatase from rat intestine

Saini, Parmesh K.; Done, J.

doi:10.1016/0005-2744(72)90974-6

Cited by 51 publications

(18 citation statements)

References 16 publications

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“…In a study on inhibitory effects of various compounds, it was reported that intestinal ALP is specially inhibited by L-phenylalanine (L-Phe), but not by L-homoarginine (L-HArg) [5,15]. However, in this study we found that there are some intestinal ALP isoenzymes inhibited by L-HArg.…”

Section: Introductioncontrasting

confidence: 54%

“…It has been reported that L-HArg is an inhibitor of ALP isoenzymes from the liver, bone and kidney, and L-Phe is a specific inhibitor of ALP isoenzymes from the intestine [5,15]. In the experiment of inhibitory effects of L-HArg on each isoenzyme, ALP of segment No.…”

Section: Discussionmentioning

confidence: 99%

“…The extraction of ALP was carried out by the method of Saini and Done [15]. The homogenates were treated with 30% (V/V) n-butanol, and the resulting suspension centrifuged at 3,000 × g for 20 min at 4°C [1,6].…”

Section: Extraction Of Alpmentioning

confidence: 99%

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Distribution and Properties of Rat Intestinal Alkaline Phosphatase Isoenzymes.

et al. 2001

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Abstract:The ALP activities and properties of rat intestine cut into 20 segments were examined, and we were able to demonstrate that the ALP activity of upper intestine is high compared to that of lower intestine. This result coincided with those of other reports. However, we newly clarified that there is an ALP isoenzyme found in the lower intestine which can be inhibited by L-homoarginine. The molecular weight of the ALP isoenzyme was 136 kDa. In addition, it was clarified that there are several isoenzymes from upper to lower intestine. This study demonstrates that there exist isoenzymes, which are inhibited by LHArg, in the intestine which are similar to the isoenzymes in the liver, bone and kidney. Key words: alkaline phosphatase (ALP), intestine, isoenzyme, L-homoarginine (L-HArg), rat by a high fat diet, ALP has been thought to be related to the absorption of fatty acid, carbohydrate, amino acid and protein from the intestine.We have found that the activities of ALP in the intestine or in serum are changed depending on the feeding conditions and have had an interest in factors which modulate the quantity of ALP protein and the activity of ALP. In a study on inhibitory effects of various compounds, it was reported that intestinal ALP is specially inhibited by L-phenylalanine (L-Phe), but not by L-homoarginine (L-HArg) [5,15]. However, in this study we found that there are some intestinal ALP isoenzymes inhibited by L-HArg. The purpose of this study was to demonstrate the properties of intestinal ALP isoenzymes by polyacrylamide gel electrophoresis (PAGE).

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Section: Introductioncontrasting

confidence: 54%

Section: Discussionmentioning

confidence: 99%

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Distribution and Properties of Rat Intestinal Alkaline Phosphatase Isoenzymes.

et al. 2001

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“…Although dual forms of human intestinal (Kelly & Alpers, 1973) and human kidney (de Burlet & Sudaka, 1976) maltases have been reported, we did not find this for the rat intestinal enzyme. Two other intestinal membrane enzymes, alkaline phosphatase (Saini & Done, 1972) and aminopeptidase (Kim & Brophy, 1976), have been shown to exist in several forms, the most likely explanation being heterogeneity of carbohydrate composition, although limited proteolysis (Malik & Butterworth, 1976) is a possibility.…”

Section: Discussionmentioning

confidence: 99%

Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH

Flanagan¹,

Forstner²

1978

Biochemical Journal

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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 enzyme was re-activated by re-adjustment of the pH to neutrality. However, in the presence of sodium dodecyl sulphate, acid pH values inactivated maltase irreversibly, and at the same time converted the enzyme (mol.wt. 500000 approx.) into five new species with apparent molecular weights ranging from 134000 to 480000 as judged by polyacrylamide-gel electrophoresis. The same five fragments were also formed by boiling the enzyme for brief periods in the presence of sodium dodecyl sulphate or urea either with or without reducing agents. The dissociated species were stable on re-electrophoresis, and amino acid analysis showed them to be very similar to each other and to the original enzyme. The bands migrated anomalously on polyacrylamide gels of different concentration, thereby preventing the assignment of precise molecular weights. It is possible that the five species may represent stable aggregates of a common monomer of the enzyme.

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“…These enzymes are now considered to represent a heterogenous group of enzymes (26,27). However, the physiologic function of these enzymes which are so abundant in the intestine have not been defined.…”

Section: Discussionmentioning

confidence: 99%