A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties

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A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties. / Danielsen, Erik Michael; Vyas, J P; Kenny, A J.

I: Biochemical Journal, Bind 191, Nr. 2, 1980, s. 645-8.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Danielsen, EM, Vyas, JP & Kenny, AJ 1980, 'A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties', Biochemical Journal, bind 191, nr. 2, s. 645-8.

APA

Danielsen, E. M., Vyas, J. P., & Kenny, A. J. (1980). A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties. Biochemical Journal, 191(2), 645-8.

Vancouver

Danielsen EM, Vyas JP, Kenny AJ. A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties. Biochemical Journal. 1980;191(2):645-8.

Author

Danielsen, Erik Michael ; Vyas, J P ; Kenny, A J. / A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties. I: Biochemical Journal. 1980 ; Bind 191, Nr. 2. s. 645-8.

Bibtex

@article{6aa956f06c8011de8bc9000ea68e967b,
title = "A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties",
abstract = "An enzyme hydrolysing [125I]iodo-insulin B chain was enriched in preparations of intestinal microvilli. The activity could be solubilized by Triton X-100 and was partially (76-fold) purified. It was very sensitive to inhibition by phosphoramidon and was also inhibited by chelating agents. In its enzymic, molecular and immunological properties the intestinal enzyme closely resembled kidney microvillar neutral endopeptidase (kidney-brush-border neutral proteinase, EC 3.4.24.11).",
author = "Danielsen, {Erik Michael} and Vyas, {J P} and Kenny, {A J}",
note = "Keywords: Animals; Cations, Divalent; Cell Membrane; Chelating Agents; Chemical Phenomena; Chemistry; Endopeptidases; Intestinal Mucosa; Microvilli; Molecular Weight; Protease Inhibitors; Swine",
year = "1980",
language = "English",
volume = "191",
pages = "645--8",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",

}

RIS

TY - JOUR

T1 - A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties

AU - Danielsen, Erik Michael

AU - Vyas, J P

AU - Kenny, A J

N1 - Keywords: Animals; Cations, Divalent; Cell Membrane; Chelating Agents; Chemical Phenomena; Chemistry; Endopeptidases; Intestinal Mucosa; Microvilli; Molecular Weight; Protease Inhibitors; Swine

PY - 1980

Y1 - 1980

N2 - An enzyme hydrolysing [125I]iodo-insulin B chain was enriched in preparations of intestinal microvilli. The activity could be solubilized by Triton X-100 and was partially (76-fold) purified. It was very sensitive to inhibition by phosphoramidon and was also inhibited by chelating agents. In its enzymic, molecular and immunological properties the intestinal enzyme closely resembled kidney microvillar neutral endopeptidase (kidney-brush-border neutral proteinase, EC 3.4.24.11).

AB - An enzyme hydrolysing [125I]iodo-insulin B chain was enriched in preparations of intestinal microvilli. The activity could be solubilized by Triton X-100 and was partially (76-fold) purified. It was very sensitive to inhibition by phosphoramidon and was also inhibited by chelating agents. In its enzymic, molecular and immunological properties the intestinal enzyme closely resembled kidney microvillar neutral endopeptidase (kidney-brush-border neutral proteinase, EC 3.4.24.11).

M3 - Journal article

C2 - 7016112

VL - 191

SP - 645

EP - 648

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -

ID: 13063926