TY - JOUR
T1 - Aspartate aminotransferase in rat tissues
T2 - Changes with growth and hormones
AU - Herzfeld, Annemarie
AU - Greengard, Olga
N1 - Funding Information:
The authors wish to thank Dr. W. Eugene Knox for helpful suggestions and Mr. Bruce B. Duncan for technical assistance. This investigation was supported by U. S. Public Health Service research grants CA 08676 from the National Cancer Institute, liD 04532 from the National Institute of Child Health and Human Development and General Research Support Grant RR 05591 from General Research Support Branch, Division of Research Resources; and by U. S. Atomic Energy Commission Contract AT(3o-1)-3779 with the New England Deaconess Hospital.
PY - 1971/4/20
Y1 - 1971/4/20
N2 - Levels of the two isozymal forms of aspartate aminotransferase (EC 2.6.1.1) were determined in normal and neoplastic rat tissues. Of the adult tissues with high total aspartate aminostransferase activity heart and muscle contain twice as much soluble than particulate isozyme while in liver and kidney (and tumors whose total activity is low) the particulate isozyme predominates. Mammary gland begins to exhibit aspartate aminotransferase activity after parturition and the soluble isozyme continues to rise throughout lactation. Fetal tissues have generally low aspartate aminotransferase activity; the different rates of its accumulation during gestation and postnatal life determined in liver, kidney and heart. The administration of thyroxine 2 days before birth, or that hydrocortisone 2 days before birth, promotes the accumulation of liver aspartate aminotransferase. Estradiol inhibits the developmental formation of the enzyme in liver and prevents the hydrocortisone induction of soluble aspartate aminostransferase in liver of adult males. The results indicate that the amounts of the two forms of aspartate aminotransferase are subject to different physiological control in different tissues. The response of the liver isozymes to hormones depends on the stage of development and after maturity of the sex of the animal.
AB - Levels of the two isozymal forms of aspartate aminotransferase (EC 2.6.1.1) were determined in normal and neoplastic rat tissues. Of the adult tissues with high total aspartate aminostransferase activity heart and muscle contain twice as much soluble than particulate isozyme while in liver and kidney (and tumors whose total activity is low) the particulate isozyme predominates. Mammary gland begins to exhibit aspartate aminotransferase activity after parturition and the soluble isozyme continues to rise throughout lactation. Fetal tissues have generally low aspartate aminotransferase activity; the different rates of its accumulation during gestation and postnatal life determined in liver, kidney and heart. The administration of thyroxine 2 days before birth, or that hydrocortisone 2 days before birth, promotes the accumulation of liver aspartate aminotransferase. Estradiol inhibits the developmental formation of the enzyme in liver and prevents the hydrocortisone induction of soluble aspartate aminostransferase in liver of adult males. The results indicate that the amounts of the two forms of aspartate aminotransferase are subject to different physiological control in different tissues. The response of the liver isozymes to hormones depends on the stage of development and after maturity of the sex of the animal.
UR - http://www.scopus.com/inward/record.url?scp=0015233550&partnerID=8YFLogxK
U2 - 10.1016/0304-4165(71)90033-X
DO - 10.1016/0304-4165(71)90033-X
M3 - Article
C2 - 4325345
AN - SCOPUS:0015233550
SN - 0304-4165
VL - 237
SP - 88
EP - 98
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 1
ER -