Tissue distribution of enzymes of arginine biosynthesis in terrestrial snails

James W. Campbell, Kermit V Speeg

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

1. The levels of activity for ornithine carbamoyltransferase (E.C. 2.1.3.3), argininosuccinate synthetase (E.C. 6.3.4.5) and argininosuccinate lyase (E.C. 4.3.2.1) were determined in various tissues of the land snails Otala lactea and Helix aspersa. The tissues examined were of endodermal, mesodermal and ectodermal origins. All tissues possessed activities of these three enzymes. 2. The levels of the three enzymes were relatively uniform from one tissue to the other with the exception of blood in which only low levels of activity were found. The lack of localization of these enzymes in any one tissue in the snails is in contrast to higher vertebrates where high levels of the arginine pathway enzymes are localized in one or very few tissues. 3. The tissue distribution of the enzymes of arginine biosynthesis in O. lactea and H. aspersa is consistent with previous studies in which it has been shown that the protein arginine in each tissue is labelled following the injection of [14C]bicarbonate into whole snails. The apparent capacity of each tissue to synthesize arginine may reflect the relative lack of differentiation of the tissues with respect to the arginine pathway in comparison to that found in mammals.

Original languageEnglish (US)
Pages (from-to)164-175
Number of pages12
JournalZeitschrift für Vergleichende Physiologie
Volume61
Issue number2
DOIs
StatePublished - Jun 1968
Externally publishedYes

Fingerprint

Snails
tissue distribution
Tissue Distribution
snail
arginine
snails
Arginine
biosynthesis
enzyme
Enzymes
enzymes
argininosuccinate lyase
ornithine carbamoyltransferase
Helix aspersa
Argininosuccinate Lyase
Argininosuccinate Synthase
Ornithine Carbamoyltransferase
tissues
distribution
tissue

ASJC Scopus subject areas

  • Behavioral Neuroscience
  • Neuroscience(all)
  • Physiology (medical)
  • Physiology
  • Animal Science and Zoology

Cite this

Tissue distribution of enzymes of arginine biosynthesis in terrestrial snails. / Campbell, James W.; Speeg, Kermit V.

In: Zeitschrift für Vergleichende Physiologie, Vol. 61, No. 2, 06.1968, p. 164-175.

Research output: Contribution to journalArticle

@article{855ca8caaecd47369b9dcfca6ae84056,
title = "Tissue distribution of enzymes of arginine biosynthesis in terrestrial snails",
abstract = "1. The levels of activity for ornithine carbamoyltransferase (E.C. 2.1.3.3), argininosuccinate synthetase (E.C. 6.3.4.5) and argininosuccinate lyase (E.C. 4.3.2.1) were determined in various tissues of the land snails Otala lactea and Helix aspersa. The tissues examined were of endodermal, mesodermal and ectodermal origins. All tissues possessed activities of these three enzymes. 2. The levels of the three enzymes were relatively uniform from one tissue to the other with the exception of blood in which only low levels of activity were found. The lack of localization of these enzymes in any one tissue in the snails is in contrast to higher vertebrates where high levels of the arginine pathway enzymes are localized in one or very few tissues. 3. The tissue distribution of the enzymes of arginine biosynthesis in O. lactea and H. aspersa is consistent with previous studies in which it has been shown that the protein arginine in each tissue is labelled following the injection of [14C]bicarbonate into whole snails. The apparent capacity of each tissue to synthesize arginine may reflect the relative lack of differentiation of the tissues with respect to the arginine pathway in comparison to that found in mammals.",
author = "Campbell, {James W.} and Speeg, {Kermit V}",
year = "1968",
month = "6",
doi = "10.1007/BF00341113",
language = "English (US)",
volume = "61",
pages = "164--175",
journal = "Journal of Comparative Physiology A: Neuroethology, Sensory, Neural, and Behavioral Physiology",
issn = "0340-7594",
publisher = "Springer Verlag",
number = "2",

}

TY - JOUR

T1 - Tissue distribution of enzymes of arginine biosynthesis in terrestrial snails

AU - Campbell, James W.

AU - Speeg, Kermit V

PY - 1968/6

Y1 - 1968/6

N2 - 1. The levels of activity for ornithine carbamoyltransferase (E.C. 2.1.3.3), argininosuccinate synthetase (E.C. 6.3.4.5) and argininosuccinate lyase (E.C. 4.3.2.1) were determined in various tissues of the land snails Otala lactea and Helix aspersa. The tissues examined were of endodermal, mesodermal and ectodermal origins. All tissues possessed activities of these three enzymes. 2. The levels of the three enzymes were relatively uniform from one tissue to the other with the exception of blood in which only low levels of activity were found. The lack of localization of these enzymes in any one tissue in the snails is in contrast to higher vertebrates where high levels of the arginine pathway enzymes are localized in one or very few tissues. 3. The tissue distribution of the enzymes of arginine biosynthesis in O. lactea and H. aspersa is consistent with previous studies in which it has been shown that the protein arginine in each tissue is labelled following the injection of [14C]bicarbonate into whole snails. The apparent capacity of each tissue to synthesize arginine may reflect the relative lack of differentiation of the tissues with respect to the arginine pathway in comparison to that found in mammals.

AB - 1. The levels of activity for ornithine carbamoyltransferase (E.C. 2.1.3.3), argininosuccinate synthetase (E.C. 6.3.4.5) and argininosuccinate lyase (E.C. 4.3.2.1) were determined in various tissues of the land snails Otala lactea and Helix aspersa. The tissues examined were of endodermal, mesodermal and ectodermal origins. All tissues possessed activities of these three enzymes. 2. The levels of the three enzymes were relatively uniform from one tissue to the other with the exception of blood in which only low levels of activity were found. The lack of localization of these enzymes in any one tissue in the snails is in contrast to higher vertebrates where high levels of the arginine pathway enzymes are localized in one or very few tissues. 3. The tissue distribution of the enzymes of arginine biosynthesis in O. lactea and H. aspersa is consistent with previous studies in which it has been shown that the protein arginine in each tissue is labelled following the injection of [14C]bicarbonate into whole snails. The apparent capacity of each tissue to synthesize arginine may reflect the relative lack of differentiation of the tissues with respect to the arginine pathway in comparison to that found in mammals.

UR - http://www.scopus.com/inward/record.url?scp=30744469429&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=30744469429&partnerID=8YFLogxK

U2 - 10.1007/BF00341113

DO - 10.1007/BF00341113

M3 - Article

AN - SCOPUS:30744469429

VL - 61

SP - 164

EP - 175

JO - Journal of Comparative Physiology A: Neuroethology, Sensory, Neural, and Behavioral Physiology

JF - Journal of Comparative Physiology A: Neuroethology, Sensory, Neural, and Behavioral Physiology

SN - 0340-7594

IS - 2

ER -