Studies on inositolphosphatase in rat small intestine

Radhakrishna Rao, C. V. Ramakrishnan

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The possibility that inositolphosphatase differs from other intestinal phosphatases was tested by comparing several enzymatic characteristics of phosphatase activities of rat intestinal homogenate acting on various specific substrates. Optimum pH and temperature, K(m), V(max), heat stability, inhibition and metal ion requirement studies suggest that inositolphosphatase differs from phytase and p-nitrophenylphosphatase. Furthermore, we found that inositolphosphatase activity was about 2 times higher in duodenum and jejunum than ileum. It sedimented (90-100%) with a high-speed particulate fraction of mucosal homogenate; 42% of the activity was separated with the brush border membrane isolated from mucosal homogenate. Partial separation by gel filtration on Sephadex G200 and chromatography on phenyl Sepharose CL 4B provided additional evidence to suggest that inositolphosphatase and phytase are different enzymes.

Original languageEnglish (US)
Pages (from-to)205-215
Number of pages11
JournalEnzyme
Volume33
Issue number4
DOIs
StatePublished - Jan 1 1985
Externally publishedYes

Fingerprint

6-Phytase
Phosphoric Monoester Hydrolases
Small Intestine
Rats
4-Nitrophenylphosphatase
Brushes
Jejunum
Microvilli
Chromatography
Ileum
Duodenum
Gel Chromatography
Metal ions
Hot Temperature
Gels
Metals
Ions
Membranes
Temperature
Substrates

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Studies on inositolphosphatase in rat small intestine. / Rao, Radhakrishna; Ramakrishnan, C. V.

In: Enzyme, Vol. 33, No. 4, 01.01.1985, p. 205-215.

Research output: Contribution to journalArticle

Rao, Radhakrishna ; Ramakrishnan, C. V. / Studies on inositolphosphatase in rat small intestine. In: Enzyme. 1985 ; Vol. 33, No. 4. pp. 205-215.
@article{7a4e261ae2e54c868bb669e99e7e6897,
title = "Studies on inositolphosphatase in rat small intestine",
abstract = "The possibility that inositolphosphatase differs from other intestinal phosphatases was tested by comparing several enzymatic characteristics of phosphatase activities of rat intestinal homogenate acting on various specific substrates. Optimum pH and temperature, K(m), V(max), heat stability, inhibition and metal ion requirement studies suggest that inositolphosphatase differs from phytase and p-nitrophenylphosphatase. Furthermore, we found that inositolphosphatase activity was about 2 times higher in duodenum and jejunum than ileum. It sedimented (90-100{\%}) with a high-speed particulate fraction of mucosal homogenate; 42{\%} of the activity was separated with the brush border membrane isolated from mucosal homogenate. Partial separation by gel filtration on Sephadex G200 and chromatography on phenyl Sepharose CL 4B provided additional evidence to suggest that inositolphosphatase and phytase are different enzymes.",
author = "Radhakrishna Rao and Ramakrishnan, {C. V.}",
year = "1985",
month = "1",
day = "1",
doi = "10.1159/000469435",
language = "English (US)",
volume = "33",
pages = "205--215",
journal = "Enzyme",
issn = "0013-9432",
number = "4",

}

TY - JOUR

T1 - Studies on inositolphosphatase in rat small intestine

AU - Rao, Radhakrishna

AU - Ramakrishnan, C. V.

PY - 1985/1/1

Y1 - 1985/1/1

N2 - The possibility that inositolphosphatase differs from other intestinal phosphatases was tested by comparing several enzymatic characteristics of phosphatase activities of rat intestinal homogenate acting on various specific substrates. Optimum pH and temperature, K(m), V(max), heat stability, inhibition and metal ion requirement studies suggest that inositolphosphatase differs from phytase and p-nitrophenylphosphatase. Furthermore, we found that inositolphosphatase activity was about 2 times higher in duodenum and jejunum than ileum. It sedimented (90-100%) with a high-speed particulate fraction of mucosal homogenate; 42% of the activity was separated with the brush border membrane isolated from mucosal homogenate. Partial separation by gel filtration on Sephadex G200 and chromatography on phenyl Sepharose CL 4B provided additional evidence to suggest that inositolphosphatase and phytase are different enzymes.

AB - The possibility that inositolphosphatase differs from other intestinal phosphatases was tested by comparing several enzymatic characteristics of phosphatase activities of rat intestinal homogenate acting on various specific substrates. Optimum pH and temperature, K(m), V(max), heat stability, inhibition and metal ion requirement studies suggest that inositolphosphatase differs from phytase and p-nitrophenylphosphatase. Furthermore, we found that inositolphosphatase activity was about 2 times higher in duodenum and jejunum than ileum. It sedimented (90-100%) with a high-speed particulate fraction of mucosal homogenate; 42% of the activity was separated with the brush border membrane isolated from mucosal homogenate. Partial separation by gel filtration on Sephadex G200 and chromatography on phenyl Sepharose CL 4B provided additional evidence to suggest that inositolphosphatase and phytase are different enzymes.

UR - http://www.scopus.com/inward/record.url?scp=0022415553&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022415553&partnerID=8YFLogxK

U2 - 10.1159/000469435

DO - 10.1159/000469435

M3 - Article

VL - 33

SP - 205

EP - 215

JO - Enzyme

JF - Enzyme

SN - 0013-9432

IS - 4

ER -