Histaminase (diamine oxidase) activity in human tumors

an expression of a mature genome

Research output: Contribution to journalArticle

Abstract

High histaminase [amine:oxygen odidoreductase (deaminating) (pyridoxal containing)] activity is found in certain human tumors and in the placenta of most mammals. This study explores the relation of tumor histaminase to histaminases found in placenta and other human, pig, and rat tissues. The electrophoretic mobility and Michaelis constants for the deamination of histamine and putrescine were identical for histaminases from human placenta and from medullary thyroid carcinoma. An antibody was raised in rabbits against human placental histaminase that was highly purified by a new affinity procedure. In separate studies, using inhibitory concentrations of antibody and a second antibody precipitation technique, identical patterns of immunoreactivity were found for histaminases from human placenta, kidney, medullary thyroid carcinoma, and small cell lung carcinoma; human intestinal histaminase cross reacted well but less strongly than did enzymes from these other tissues. Histaminases from pig kidney, pig intestine, and rat intestine showed no cross reaction; histaminases from rat thymus and adrenal gland showed minimal cross reactivity. The findings suggest that placental histaminase activity is not a unique product of a fetal or trophoblastic genome. The presence of histaminase in cancers does not appear to be an example of ectopic tumor production of a placental trophoblastic protein.

Original languageEnglish (US)
Pages (from-to)883-887
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume74
Issue number3
StatePublished - 1977

Fingerprint

Amine Oxidase (Copper-Containing)
Human Activities
Genome
Neoplasms
Placenta
Swine
Intestines
Antibodies
Pyridoxal
Pregnancy Proteins
Kidney
Deamination
Putrescine
Cross Reactions
Small Cell Lung Carcinoma
Adrenal Glands
Thymus Gland
Histamine
Amines
Mammals

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

@article{fed18d1aac1f4ae9a99a488c0e692b43,
title = "Histaminase (diamine oxidase) activity in human tumors: an expression of a mature genome",
abstract = "High histaminase [amine:oxygen odidoreductase (deaminating) (pyridoxal containing)] activity is found in certain human tumors and in the placenta of most mammals. This study explores the relation of tumor histaminase to histaminases found in placenta and other human, pig, and rat tissues. The electrophoretic mobility and Michaelis constants for the deamination of histamine and putrescine were identical for histaminases from human placenta and from medullary thyroid carcinoma. An antibody was raised in rabbits against human placental histaminase that was highly purified by a new affinity procedure. In separate studies, using inhibitory concentrations of antibody and a second antibody precipitation technique, identical patterns of immunoreactivity were found for histaminases from human placenta, kidney, medullary thyroid carcinoma, and small cell lung carcinoma; human intestinal histaminase cross reacted well but less strongly than did enzymes from these other tissues. Histaminases from pig kidney, pig intestine, and rat intestine showed no cross reaction; histaminases from rat thymus and adrenal gland showed minimal cross reactivity. The findings suggest that placental histaminase activity is not a unique product of a fetal or trophoblastic genome. The presence of histaminase in cancers does not appear to be an example of ectopic tumor production of a placental trophoblastic protein.",
author = "Baylin, {Stephen B}",
year = "1977",
language = "English (US)",
volume = "74",
pages = "883--887",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "3",

}

TY - JOUR

T1 - Histaminase (diamine oxidase) activity in human tumors

T2 - an expression of a mature genome

AU - Baylin, Stephen B

PY - 1977

Y1 - 1977

N2 - High histaminase [amine:oxygen odidoreductase (deaminating) (pyridoxal containing)] activity is found in certain human tumors and in the placenta of most mammals. This study explores the relation of tumor histaminase to histaminases found in placenta and other human, pig, and rat tissues. The electrophoretic mobility and Michaelis constants for the deamination of histamine and putrescine were identical for histaminases from human placenta and from medullary thyroid carcinoma. An antibody was raised in rabbits against human placental histaminase that was highly purified by a new affinity procedure. In separate studies, using inhibitory concentrations of antibody and a second antibody precipitation technique, identical patterns of immunoreactivity were found for histaminases from human placenta, kidney, medullary thyroid carcinoma, and small cell lung carcinoma; human intestinal histaminase cross reacted well but less strongly than did enzymes from these other tissues. Histaminases from pig kidney, pig intestine, and rat intestine showed no cross reaction; histaminases from rat thymus and adrenal gland showed minimal cross reactivity. The findings suggest that placental histaminase activity is not a unique product of a fetal or trophoblastic genome. The presence of histaminase in cancers does not appear to be an example of ectopic tumor production of a placental trophoblastic protein.

AB - High histaminase [amine:oxygen odidoreductase (deaminating) (pyridoxal containing)] activity is found in certain human tumors and in the placenta of most mammals. This study explores the relation of tumor histaminase to histaminases found in placenta and other human, pig, and rat tissues. The electrophoretic mobility and Michaelis constants for the deamination of histamine and putrescine were identical for histaminases from human placenta and from medullary thyroid carcinoma. An antibody was raised in rabbits against human placental histaminase that was highly purified by a new affinity procedure. In separate studies, using inhibitory concentrations of antibody and a second antibody precipitation technique, identical patterns of immunoreactivity were found for histaminases from human placenta, kidney, medullary thyroid carcinoma, and small cell lung carcinoma; human intestinal histaminase cross reacted well but less strongly than did enzymes from these other tissues. Histaminases from pig kidney, pig intestine, and rat intestine showed no cross reaction; histaminases from rat thymus and adrenal gland showed minimal cross reactivity. The findings suggest that placental histaminase activity is not a unique product of a fetal or trophoblastic genome. The presence of histaminase in cancers does not appear to be an example of ectopic tumor production of a placental trophoblastic protein.

UR - http://www.scopus.com/inward/record.url?scp=0017364524&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017364524&partnerID=8YFLogxK

M3 - Article

VL - 74

SP - 883

EP - 887

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 3

ER -