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HAYASHI, MASANDO; FREIMAN, DAVID G.
doi: 10.1177/14.8.577pmid: 4165546
Studies have been made on the effect of fixatives containing substrate and other additives on the histochemical staining reaction for myosin adenosine triphosphatase activity in the leg muscle, and α-glycerophosphate and succinate dehydrogenase activities in the kidney of the rat. Myosin adenosine triphosphatase was well preserved in the presence of adenosine triphosphate in fixative prepared from methanol-free formaldehyde and buffered to pH 7.2 with cacodylate. Addition of sucrose was found to increase the enzyme preservation. Similar protection of the enzyme activity was afforded by other polyphosphates, particularly sodium pyrophosphate and, to less degree, thiamine pyrophosphate, adenosine diphosphate and uridine triphosphate. α-Glycerophosphate dehydrogenase was also preserved to greater degree by a similar fixative containing α-glycerophosphate than by substrate-free fixative. Succinate dehydrogenase was not significantly preserved in succinate-containing fixative. On the other hand, sucrose in the fixative increased the preservation of succinate dehydrogenase but had no appreciable effect on α-glycerophosphate dehydrogenase.
doi: 10.1177/14.8.582pmid: 5969506
A quantitative and histochemical study of phosphorylase has been made in the human, rat and rabbit placentae. The placental enzyme was found to have the same optimal pH as liver phosphorylase. Since cyclic 3',5'-AMP, glucagon or adrenaline had no influence on enzyme activity, phosphorylase probably exists only in the active form in the placenta. The activity of phosphorylase was localized histochemically in the decidua basalis, the cytotrophoblast of the spongy zone of the chorioallantoic placenta and in the visceral layer of the inverted yolk sac of the rat. It was present mainly in the decidua basalis of placenta of the rabbit although a few cytotrophoblastic cells of the trophoblastic tubules also showed weak activity. In the human placenta the enzyme was active in the cytotrophoblast and the mesodermal core of the villi. It was present occasionally in the syncytiotrophoblast. The quantity of the enzyme fluctuates during gestation in both the human and rat fetal placentae. These fluctuations do not appear to bear relation to either placental glycogen level or to fetal liver phosphorylase activity. Nor is there any obvious correlation between placental phosphorylase and the activity of glucagon-like substance of the fetal pancreas.
BEATTY, C. H.; BASINGER, G. M.; DULLY, C. C.; BOCEK, R. M.
doi: 10.1177/14.8.590pmid: N/A
There was a direct correlation between the qualitative histochemical classification by staining intensity for succinic dehydrogenase and the quantitative measurements of succinic dehydrogenase activity for the quadratus femoris (red), soleus (red), sartorius (predominantly red) and the superficial portion of the brachioradialis (predominantly white) muscles of the rhesus monkey. The relative succinic dehydrogenase activities were quadratus femoris > soleus > sartorius > brachioradialis, the quadratus femoris having 7 times more enzyme activity than the brachioradialis. The sartorius of male rhesus monkeys had a higher enzyme activity than that of the female. Muscle samples were stained with sirius red and graded for amounts of connective tissue as follows: soleus < sartorius < brachioradialis. These histochemical results were verified by chemical analyses. The soleus, sartorius and brachioradialis from 10 other species of primates had the same relative succinic dehydrogenase activities and histochemical staining patterns as the rhesus.
DECOSSE, JEROME J.; AIELLO, NANCY
doi: 10.1177/14.8.601pmid: 5969507
Two methods of Feulgen hydrolysis (5.0 N HCl at room temperature and 1.0. N HCl at 60°C) were examined by serial microspectrophotometric measurements of the relative DNA content of normal human lymphocytes subjected to each hydrolysis. The DNA contents at optimum hydrolysis were equal by both methods. Hydrolysis in 5.0 N HCl at room temperature resulted in an interval of 120 min of stable peak values. Successive hydrolyses to the optimum time, as defined for each methtod in the initial experiment, indicated that hydrolysis 5.0. N HCl at room temperature provided a more reliable technique. The results also suggested that depurination is dependent primarily on acid rather than heat, while further degradation is dependent primarily on heat rather than acid.
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