Characterisation of a novel proteolytic enzyme localised to goblet cells in rat and man

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Characterisation of a novel proteolytic enzyme localised to goblet cells in rat and man. / Poulsen, Steen Seier.

In: Gut, Vol. 25, No. 6, 06.1984, p. 656-64.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Poulsen, SS 1984, 'Characterisation of a novel proteolytic enzyme localised to goblet cells in rat and man', Gut, vol. 25, no. 6, pp. 656-64.

APA

Poulsen, S. S. (1984). Characterisation of a novel proteolytic enzyme localised to goblet cells in rat and man. Gut, 25(6), 656-64.

Vancouver

Poulsen SS. Characterisation of a novel proteolytic enzyme localised to goblet cells in rat and man. Gut. 1984 Jun;25(6):656-64.

Author

Poulsen, Steen Seier. / Characterisation of a novel proteolytic enzyme localised to goblet cells in rat and man. In: Gut. 1984 ; Vol. 25, No. 6. pp. 656-64.

Bibtex

@article{7ae0df0213b44603a741fd4c84555d9e,
title = "Characterisation of a novel proteolytic enzyme localised to goblet cells in rat and man",
abstract = "A proteolytic enzyme, ingobsin , purified from rat duodenal extracts is shown to be localised to intestinal goblet cells of both man and rat. Enzyme positive cells decrease in number from duodenum to colon. The enzyme is a 33 000 Mr protein with an isoelectric point of 5.1. The pH optimum for enzymatic activity is 7.4-8.0. Based on substrate specificity for arg-x, lys-x and to a lesser degree tyr-x, on the effect of diisopropylphosphorofluoride , Trasylol and phenylmethylsulfonylfluoride and on proteolytic activity towards intact proteins, ingobsin is classified as a serine proteinase with endoproteolytic activity.",
keywords = "Animals, Humans, Hydrogen-Ion Concentration, Intestinal Mucosa, Isoelectric Point, Molecular Weight, Rats, Rats, Inbred Strains, Substrate Specificity",
author = "Poulsen, {Steen Seier}",
year = "1984",
month = jun,
language = "English",
volume = "25",
pages = "656--64",
journal = "Gut",
issn = "0017-5749",
publisher = "B M J Group",
number = "6",

}

RIS

TY - JOUR

T1 - Characterisation of a novel proteolytic enzyme localised to goblet cells in rat and man

AU - Poulsen, Steen Seier

PY - 1984/6

Y1 - 1984/6

N2 - A proteolytic enzyme, ingobsin , purified from rat duodenal extracts is shown to be localised to intestinal goblet cells of both man and rat. Enzyme positive cells decrease in number from duodenum to colon. The enzyme is a 33 000 Mr protein with an isoelectric point of 5.1. The pH optimum for enzymatic activity is 7.4-8.0. Based on substrate specificity for arg-x, lys-x and to a lesser degree tyr-x, on the effect of diisopropylphosphorofluoride , Trasylol and phenylmethylsulfonylfluoride and on proteolytic activity towards intact proteins, ingobsin is classified as a serine proteinase with endoproteolytic activity.

AB - A proteolytic enzyme, ingobsin , purified from rat duodenal extracts is shown to be localised to intestinal goblet cells of both man and rat. Enzyme positive cells decrease in number from duodenum to colon. The enzyme is a 33 000 Mr protein with an isoelectric point of 5.1. The pH optimum for enzymatic activity is 7.4-8.0. Based on substrate specificity for arg-x, lys-x and to a lesser degree tyr-x, on the effect of diisopropylphosphorofluoride , Trasylol and phenylmethylsulfonylfluoride and on proteolytic activity towards intact proteins, ingobsin is classified as a serine proteinase with endoproteolytic activity.

KW - Animals

KW - Humans

KW - Hydrogen-Ion Concentration

KW - Intestinal Mucosa

KW - Isoelectric Point

KW - Molecular Weight

KW - Rats

KW - Rats, Inbred Strains

KW - Substrate Specificity

M3 - Journal article

C2 - 6735249

VL - 25

SP - 656

EP - 664

JO - Gut

JF - Gut

SN - 0017-5749

IS - 6

ER -

ID: 47489307