The measurement of nucleic acid turnover in rat liver

Swick, Robert W.; Koch, Arthur L.; Handa, Dorothy T.

doi:10.1016/0003-9861(56)90026-1

Cited by 58 publications

(30 citation statements)

References 17 publications

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“…Albumin synthesis was determined by the injection of carbonate-14C with its subsequent incorporation into the guanido carbon of arginine and, hence, into albumin. The specific activity of the carbon of urea was taken to represent that of the precursor guanido carbon of arginine as described previously (8)(9)(10).…”

Section: Methods (A) Whole Animal Studiesmentioning

confidence: 99%

“…These spaces (measured from the space of distribution of urea-14C) were determined to be about 60%o. The specific activity of this urea carbon was assumed to equal the mean specific activity of the precursor guanido carbon of arginine (8)(9)(10). The concentration of protein in plasma or perfusate was determined with a biuret-reagent (17) and protein partition with a Kern microelectrophoresis unit (18).…”

Section: Methods (A) Whole Animal Studiesmentioning

confidence: 99%

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Effects of a short-term fast on albumin synthesis studied in vivo, in the perfused liver, and on amino acid incorporation by hepatic microsomes

Rothschild¹,

Oratz²,

Mongelli³

et al. 1968

J. Clin. Invest.

124

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AB S TRA CT Carbonate-14C was used to label the hepatic intracellular arginine pool and direct measurement of albumin synthesis was made in six rabbits before and after an 18-36 hr fast. 18 perfusion studies were performed with livers derived from fed and fasted rabbits (18-24 hr). Microsomal amino acid-incorporating ability with leucine-MH and phenylalanine-14C was compared in 17 studies, using microsomes isolated from livers taken from fed and fasted rabbits and from isolated perfused livers whose donors were fed and fasted.Albumin synthesis is rapidly inhibited by fasting. Albumin synthesis decreased 337%o in vivo and 53%o in the perfused liver. The microsomes from perfused livers taken from fed animals did not demonstrate a significantly reduced capacity to incorporate leucine-3H or phenylalanine-'4C into protein. Microsomes derived from perfused and nonperfused livers whose donors were fasted incorporated 32-54%o less tracer than microsomes obtained from fed donor rabbits. Microsomes separated from perfused livers removed from fed and fasted rabbits responded to polyuridylic acid stimulation and phenylalanine-14C incorporation rose from 58 to 171%. An 18-36 hr fast inhibits albumin production in vivo and in the perfused liver. The microsomal

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Section: Methods (A) Whole Animal Studiesmentioning

confidence: 99%

Section: Methods (A) Whole Animal Studiesmentioning

confidence: 99%

Effects of a short-term fast on albumin synthesis studied in vivo, in the perfused liver, and on amino acid incorporation by hepatic microsomes

Rothschild¹,

Oratz²,

Mongelli³

et al. 1968

J. Clin. Invest.

124

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“…The latter observation suggests that in some patients with severe liver disease and ascites albumin synthesis may be increased and the low serum level may reflect dilution and altered distribution. The introduction of a method which permits the study of albumin production over a period of a few hours has permitted the examination of albumin production in acutely ill patients who cannot be expected to remain in the steady state for more than a few hours to say nothing of the days or weeks required to follow the degradation of exogenously labeled albumin (9)(10)(11). This report describes the measurement of albumin synthesis by endogenous labeling of albumin with carbonate-14C in 19 subjects with liver disease and massive ascites associated with alcoholism, and demonstrates that in Tables I and II. (13).…”

Section: Introductionmentioning

confidence: 99%

Albumin synthesis in cirrhotic subjects with ascites studied with carbonate-14C

Rothschild¹,

Oratz²,

Zimmon³

et al. 1969

J. Clin. Invest.

138

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“…The half-life of enzymes in the liver has been estimated at 3 days while the life span of liver cells may be on the order of months (6,9). Some plant enzymes are known to be short-lived.…”

mentioning

confidence: 99%

An Invertase Inactivator in Maize Endosperm and Factors Affecting Inactivation

Jaynes

Nelson

1971

Plant Physiol.

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ases by specific proteins present in plants as well as animals. Other enzymes besides proteinases can be inhibited by proteins. A protein inhibitor of potato invertase was detected when an inhibitor-containing enzyme extract exhibited a nonlinear increase in activity with a linear increase in protein concentration. It was proposed that inhibition occurs by irreversible binding of the inhibitor to the enzyme; inhibition was noncompetitive. A metabolic role for the inhibitor was suggested when large amounts of the inhibitor and low invertase activity were found in tubers stored at 18 C and the reverse at 4 C (3-5).

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The measurement of nucleic acid turnover in rat liver

Cited by 58 publications

References 17 publications

Effects of a short-term fast on albumin synthesis studied in vivo, in the perfused liver, and on amino acid incorporation by hepatic microsomes

Effects of a short-term fast on albumin synthesis studied in vivo, in the perfused liver, and on amino acid incorporation by hepatic microsomes

Albumin synthesis in cirrhotic subjects with ascites studied with carbonate-14C

An Invertase Inactivator in Maize Endosperm and Factors Affecting Inactivation

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