Human and porcine immunoreactive gastric inhibitory polypeptides (IR-GIP) are not identical

A. J. Bacarese-Hamilton; T. E. Adrian; S. R. Bloom

doi:10.1016/0014-5793(84)80220-3

Human and porcine immunoreactive gastric inhibitory polypeptides (IR-GIP) are not identical

A. J. Bacarese-Hamilton
, T. E. Adrian
, S. R. Bloom

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

Immunoreactive gastric inhibitory polypeptide (IR-GIP) from human and porcine intestine was quantified by radioimmunoassay and the molecular forms characterised by gel permeation and reverse-phase high pressure liquid chromatography (HPLC). Gel filtration revealed two major immunoreactive peaks corresponding to the previously described 5-kDa and 8-kDa molecular forms, which appeared similar in both species. Isocratic reverse-phase HPLC revealed that the major immunoreactive GIP peak (5-kDa) in the human tissue eluted earlier than the corresponding porcine molecular form, indicating the latter to be less hydrophobic. These findings suggest significant species differences between human and porcine GIP.

Original language	English
Pages (from-to)	125-128
Number of pages	4
Journal	FEBS Letters
Volume	168
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(84)80220-3
Publication status	Published - Mar 12 1984
Externally published	Yes

Keywords

Gastric inhibitory polypeptide
Gel filtration
Glucose-dependent insulinotropic peptide
Immunoreactive GIP
Molecular form
Reverse-phase HPLC
Species difference

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(84)80220-3

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title = "Human and porcine immunoreactive gastric inhibitory polypeptides (IR-GIP) are not identical",

abstract = "Immunoreactive gastric inhibitory polypeptide (IR-GIP) from human and porcine intestine was quantified by radioimmunoassay and the molecular forms characterised by gel permeation and reverse-phase high pressure liquid chromatography (HPLC). Gel filtration revealed two major immunoreactive peaks corresponding to the previously described 5-kDa and 8-kDa molecular forms, which appeared similar in both species. Isocratic reverse-phase HPLC revealed that the major immunoreactive GIP peak (5-kDa) in the human tissue eluted earlier than the corresponding porcine molecular form, indicating the latter to be less hydrophobic. These findings suggest significant species differences between human and porcine GIP.",

keywords = "Gastric inhibitory polypeptide, Gel filtration, Glucose-dependent insulinotropic peptide, Immunoreactive GIP, Molecular form, Reverse-phase HPLC, Species difference",

author = "Bacarese-Hamilton, \{A. J.\} and Adrian, \{T. E.\} and Bloom, \{S. R.\}",

year = "1984",

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day = "12",

doi = "10.1016/0014-5793(84)80220-3",

language = "English",

volume = "168",

pages = "125--128",

journal = "FEBS Letters",

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TY - JOUR

T1 - Human and porcine immunoreactive gastric inhibitory polypeptides (IR-GIP) are not identical

AU - Bacarese-Hamilton, A. J.

AU - Adrian, T. E.

AU - Bloom, S. R.

PY - 1984/3/12

Y1 - 1984/3/12

N2 - Immunoreactive gastric inhibitory polypeptide (IR-GIP) from human and porcine intestine was quantified by radioimmunoassay and the molecular forms characterised by gel permeation and reverse-phase high pressure liquid chromatography (HPLC). Gel filtration revealed two major immunoreactive peaks corresponding to the previously described 5-kDa and 8-kDa molecular forms, which appeared similar in both species. Isocratic reverse-phase HPLC revealed that the major immunoreactive GIP peak (5-kDa) in the human tissue eluted earlier than the corresponding porcine molecular form, indicating the latter to be less hydrophobic. These findings suggest significant species differences between human and porcine GIP.

AB - Immunoreactive gastric inhibitory polypeptide (IR-GIP) from human and porcine intestine was quantified by radioimmunoassay and the molecular forms characterised by gel permeation and reverse-phase high pressure liquid chromatography (HPLC). Gel filtration revealed two major immunoreactive peaks corresponding to the previously described 5-kDa and 8-kDa molecular forms, which appeared similar in both species. Isocratic reverse-phase HPLC revealed that the major immunoreactive GIP peak (5-kDa) in the human tissue eluted earlier than the corresponding porcine molecular form, indicating the latter to be less hydrophobic. These findings suggest significant species differences between human and porcine GIP.

KW - Gastric inhibitory polypeptide

KW - Gel filtration

KW - Glucose-dependent insulinotropic peptide

KW - Immunoreactive GIP

KW - Molecular form

KW - Reverse-phase HPLC

KW - Species difference

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DO - 10.1016/0014-5793(84)80220-3

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C2 - 6705918

AN - SCOPUS:0021760910

SN - 0014-5793

VL - 168

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JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Human and porcine immunoreactive gastric inhibitory polypeptides (IR-GIP) are not identical

Abstract

Keywords

ASJC Scopus subject areas

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