Activity of lysosomal enzymes in murine mammary tissue through pregnancy, lactation, and involution.
Murine mammary tissue homogenates obtained during pregnancy, lactation, and involution were assayed for activities of two lysosomal marker enzymes, acid phosphatase, and N-acetyl-beta-D-glucosaminidase. Acid phosphatase activity per milligram protein was relatively constant through pregnancy and lactation, although a decrease was detected at parturition. Acid phosphatase activity per milligram deoxyribonucleic acid was also stable through pregnancy and lactation except for a peak of activity during lactogenesis. Acid phosphatase activity per gram wet weight also remained stable during pregnancy and lactation, but activity was significantly higher during lactation than pregnancy. Glucosaminidase activity, whether expressed as milligrams deoxyribonucleic acid of milligrams protein, tended to decrease during pregnancy, decreased further with lactogenesis, and remained significantly lower throughout lactation. Glucosaminidase activity per gram wet weight increased as pregnancy progressed and slowly decreased through lactogenesis to midpregnancy levels, which remained stable throughout the remainder of lactation. Both acid phosphatase and glucosaminidase activities were slightly higher at the end of lactation, and both decreased within 24 h of weaning. Significant increases in activities of both enzymes were observed from d 1 to 4 of involution.
D000118:Acetylglucosaminidase / Q000378:metabolism; D000135:Acid Phosphatase / Q000378:metabolism; D000704:Analysis of Variance; D000818:Animals; D005260:Female; D007774:Lactation; D008247:Lysosomes / Q000201:enzymology*; D008321:Mammary Glands, Animal / Q000201:enzymology*; D051379:Mice; D011247:Pregnancy; D011270:Pregnancy, Animal
D000135:Acid Phosphatase; D000118:Acetylglucosaminidase