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Biomedical subjects

G H WHIPPLE

Publications and source records attributed to G H WHIPPLE.

At least 37 records · Page 2Linked to original sources
PubMed1958

Vitamin B12Co60 distribution in dog tissues during many months; red cell stroma with labeled B12 in hemolytic anemia.

Experiments dealing with the distribution of B(12)Co(60) in the dog indicate that with time (9 months after administration) there is a shift in the distribution of the vitamin as compared to the short term experiments, as well as prolonged retention of the vitamin within various dog tissues. The heart, gastric mucosa, liver, spleen, and brain show high concentrations of the isotope in long term experiments. This distribution, in the heart for example, does not fit with an hypothetical breakdown of B(12)Co(60) complex and storage of a physiologically inactive fraction. Repeated periods of anemia produced by phenylhydrazine make it possible to demonstrate radioactive material in red cell stroma of dogs that have previously received vitamin B(12)Co(60). This radioactive material must have come from other body stores, such as liver and stomach. The high concentration of B(12)Co(60) in the gastric mucosa suggests a relationship between it and the intrinsic factor as described by Castle.

Anemia↗
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↗
PubMed1952

Albumin and globulin circulation in experimental ascites; relative rates of interchange between plasma and ascitic fluid studied with C14-labeled proteins.

Plasma containing carbon(14)-labeled albumin and globulin, obtained by feeding epsilon-C(14)D,L.-lysine to a donor dog, has been injected intravenously and intraperitoneally into recipient dogs with experimental ascites. The circulation and interchange of total plasma protein between circulating blood and ascitic fluid have been confirmed and the participation of both albumin and globulin in this interchange has been demonstrated. Labeled albumin tends to reach equilibrium in plasma and ascitic fluid in a shorter period of time (1 to 2 days) than does globulin (2 or more days), after administration of labeled plasma by either route. Evidence is presented that the rate of transfer of albumin across the peritoneal membrane is at least three times faster than that of globulin in terms of weight.

Albumins↗
PubMed1952

Plasma protein labeled with lysine-epsilon-C14; its oral feeding and related protein metabolism in the dog.

The metabolism of homologous plasma proteins, labeled with lysine-epsilon-C(14), after oral administration to dogs has been investigated. The speed of the various processes involved is indicated by the maximum rate of C(14) O(2) excretion which is attained within 1 to 4 hours, the prompt appearance of protein activity in the plasma and disappearance of non-protein activity from it, both virtually complete in 7 to 10 hours, as well as the rapid incorporation of a large percentage of the fed-C(14) into tissues. There are no essential differences between the behavior of labeled plasma and that of an amino acid digest containing epsilon-C(14) labeled lysine when these two materials are given orally. At the end of 48 hours after labeled plasma feeding, a CO(2) elimination of 16 to 28 per cent of the fed C(14) is noted. In contrast, after 48 hours following labeled plasma by vein, a CO(2) elimination of only 2.5 per cent is recorded-almost a 10 to 1 ratio. We believe this, together with the data concerning plasma and tissue protein activity, represents a significant difference in the metabolic process. The evidence favors a complete breakdown of plasma protein to the amino acid level when given orally but not when given by vein.

Amino Acids↗
PubMed1951

Conversion of plasma protein to tissue protein without evidence of protein breakdown; results of giving plasma protein labeled with carbon 14 parenterally to dogs.

Labeled plasma proteins obtained from donor dogs, previously fed epsilon-C(14)-dl-lysine, have been given intravenously to recipient dogs. The disappearance of labeled globulin from the plasma at a rate considerably faster than albumin has been confirmed. Evidence suggesting that the mass of protein in solution in the extravascular, extracellular fluid is approximately equal to the plasma proteins in circulation has been derived from a study of the dilution of labeled plasma protein by repeated injections of non-labeled plasma protein. In a period of 7 days the transfer of C(14) from plasma to tissue proteins amounted to between 30 and 40 per cent of the activity in the labeled plasma protein injected intravenously. The conversion was accompanied by a very small loss of activity in the urine and expired air and the activity remained in the lysine residue of the liver and probably of other tissues. The data presented favor the view that plasma proteins are utilized in the body economy after partial catabolism within the cell area and provide no evidence of complete breakdown to the amino acid level.

Amino Acids↗