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G H WHIPPLE

Publications and source records attributed to G H WHIPPLE.

29 records · Page 2Linked to original sources
PubMed1955

Stroma protein and stroma lipides vary in different types of anemia.

Normal red blood cells in dogs contain stroma in fairly uniform amounts. This red cell stroma is rich in proteins and lipides. Anemia due to blood loss causes an increase in stroma protein. The highest levels of stroma protein are found in the severe anemias. As the anemia is corrected by red cell regeneration, the stroma protein level falls to normal. Anemia due to blood destruction (phenylhydrazine) presents very high levels of stroma protein-almost double the increase noted in anemia due to blood loss. Hypoproteinemia added to anemia due to blood loss causes no significant change on the stroma protein level. Abscesses due to the subcutaneous injection of turpentine during the anemia cause slight decreases in the stroma protein levels. Chloroform poisoning has no effect on the stroma protein levels. The total lipides of the stroma are rather stable and are little influenced by anemia. In certain experiments with hemolytic anemia and with hypoproteinemia, there is a significant rise in total lipide figures.

Anemia↗
PubMed1955

Red cell stroma and hemoglobin metabolism in anemic dogs; regeneration of red cell proteins labeled with C14 lysine.

Red cell stroma protein and hemoglobin can be labeled by feeding C(14) lysine during periods of active blood regeneration following anemia. Stroma proteins are produced and a maximum concentration of the C(14) label appears 2 to 3 days earlier than with hemoglobin,-which is to say that stroma building precedes hemoglobin construction. The concentration of isotope in stroma protein may exceed its concentration in hemoglobin during regeneration following anemia due to blood loss. Diets favorable for hemoglobin regeneration may force the hemoglobin isotope concentration above that of the stroma protein. In hemolytic anemias great reserves of red cell building material are stored in the body. These stores may modify the curves of isotope concentration in red cells during the recovery periods. When finally formed, the mature red cells show little or no evidence of participation in general body protein metabolism during their life in the circulation.

Anemia↗
PubMed1955

Red cell stroma protein rich in vitamin B12 during active regeneration; anemia studies using radioactive cobalt B12 in dogs.

During active blood regeneration in anemia in dogs an increase occurs in the stroma protein of the red cells. When vitamin B(12) with radioactive cobalt is given at the start of this blood regeneration one finds concentration of labeledB(12)in the stroma protein but not in the hemoglobin. After the acute phase of red cell regeneration is ended the concentration of B(12) in stroma protein falls rapidly to very low levels within 2 weeks. Subsequent episodes of red blood cell regeneration seems not to cause remobilization of radioactive cobalt into red cells from other body stores. It appears that the vitamin B(12) is a factor of importance in the first steps of stroma protein formation in the first few days of the life of the red cell in the dog. This response in dogs and the response in pernicious anemia to vitamin B(12) may have some points in common. Distribution of the B(12)-radioactive cobalt in the organs and tissues at autopsy has been recorded. Some very suggestive localizations were noted and some variation 1 week and 7 weeks after B(12) injections. Radioactive cobalt escapes in the urine during the weeks following B(12) injections.

Anemia↗
PubMed1955

The placenta and protein metabolism; transfer studies using carbon 14-labeled proteins in dogs.

Plasma proteins tagged in vivo by feeding D-L-lysine-epsilon-C(14) to donor dogs have been administered to pregnant dogs by both oral and intravenous routes. A relatively small percentage of the C(14) activity originally incorporated in these proteins is found to pass from mother to fetus after intravenous injection. The amount transferred tends to increase with the length of gestation period and total number of fetuses. Plasma protein labeled with I(131) does not cross the placenta in the dog, but does in the rabbit. Evans blue dye does not cross the placenta of the dog. After oral administration of labeled plasma protein or lysine, C(14) is transferred promptly and in considerable quantity to the fetus. Labeled plasma proteins disappear more rapidly from the circulation of pregnant than of normal dogs. This increased metabolic turnover occurs without excretion of any excess waste metabolites. The chorionic epithelium, gram for gram, is probably 2 to 3 times as active as the hepatic epithelium in protein metabolism. These findings indicate an important placental function related to maternal and fetal protein metabolism. While the placenta utilizes maternal plasma proteins and amino acids, in a quantitative sense the latter appear to supply the major nitrogen needs of the growing fetus.

Amino Acids↗
PubMed1953

Inflammation and protein metabolism studies of carbon-14-labeled proteins in dogs with sterile abscesses.

Carbon-14-labeled plasma proteins given by mouth to dogs with sterile abscesses undergo decreased absorption, presumably owing to impaired digestion of protein. The turnover of plasma albumin is greatly accelerated but the globulins, excluding fibrinogen, show little change during the acute stage of the sterile inflammation. Fibrinogen shows very rapid production and utilization during acute inflammation. Large amounts of C(14) are incorporated in fibrinogen within a few hours after ingestion of the labeled material. The labeled fibrinogen largely disappears within 2 to 4 days after its production. The appearance of C(14) in new red cells from labeled protein or amino acid sources is reduced by inflammation-evidence of impaired synthesis. The pus of the sterile abscess contains a good deal of C(14) activity which at times is as much as that found in the liver. Pus cell C(14) activity per milliliter is similar after injection of labeled plasma and ingestion of labeled plasma or lysine. However, the pus cell fraction contains 3 to 4 times more C(14) activity per milliliter than does the supernatant fluid when the isotope is fed. In the supernatant fluid the activity is all within precipitable protein, much of which is probably derived from the blood plasma. In spite of increased loss of C(14) as CO(2) in the expired air and in the pus, there is evidence of conservation of protein-building materials for maintenance of new plasma proteins and tissue proteins in the more active organs (e.g. liver)-a shift of protein C(14) from the less active tissues (muscle and skin).

Abscess↗