Distribution of a basic azo-dye-binding protein in normal rat tissues anc carcinogen-induced hepatomata

Baldwin, Robert; Barker, C. R.; Moore, M. R.

doi:10.1038/bjc.1968.92

Cited by 17 publications

(9 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Bannikov et al [12] did not detect ligandin in water extracts of many rat tissues including spleen, lung, pancreas, myocardium, skeletal muscle and brain. The amount of ligandin determined semiquantitatively in the cell sap of rat liver was found to be significantly reduced in primary hepatomas induced by several dif ferent carcinogens [13].…”

Section: Resultsmentioning

confidence: 92%

Ligandin Content of Normal and Carcinogen-Treated Rat Tissues

Carruthers¹,

Baumler²

1980

Oncology

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 92%

Ligandin Content of Normal and Carcinogen-Treated Rat Tissues

Carruthers¹,

Baumler²

1980

Oncology

View full text Add to dashboard Cite

show abstract

“…Other compounds, such as certain carcinogens, bind covalently which may protect the cell against carcinogenesis (29,30) or may be important in promoting carcinogenesis (15,30). The concentration of the binding protein is very low in hepatomas (15,31).…”

Section: Methodsmentioning

confidence: 99%

Immunological Studies of Y Protein. A MAJOR CYTOPLASMIC ORGANIC ANION-BINDING PROTEIN IN RAT LIVER

Fleischner¹,

Robbins²,

Arias³

1972

J. Clin. Invest.

131

View full text Add to dashboard Cite

A B S T R A C T An antibody METHODSSupernatant fractions were prepared from homogenates of liver and 16 other tissues from 32 adult Sprague-Dawley, 2 Long-Evans, and 2 Gunn (glucuronyltransferase-deficient) (12) rats of either sex. Supernatant fractions were also obtained from at least two specimens of liver from Hartley guinea pigs, albino mice, Rhesus monkeys, Shetland ponies, chickens, rabbits, four species of fish, five species of amphibia, and four species of reptiles. Histologically normal human liver was obtained within 4 hr after patients died from acute myocardial infarction. All laboratory animals were anesthetized with ether and killed immediately; fishes, reptiles, and amphibia were anesthetized with urethane; and horses were killed by captive-bolt after curare administration. Various tissues were rapidly removed, perfused, where possible, with ice-cold 0.9%o saline, and a 25%o homogenate was prepared in 0.25 M sucrose-0.01 M phosphate buffer, pH 7.4, using a motor-driven, teflon pestle, glass homogenizer (Arthur H. Thomas Co., Philadelphia, Pa.). Kidney and muscle required initial disruption in a VirTis (The VirTis Co., Gardiner, N. Y.) homogenizer. Small intestine was removed from duodenum to terminal ileum, washed with cold 0.9% saline, opened lengthwise, and the mucosa was scraped between two glass slides. Blood was collected and permitted to clot at room temperature; sera were stored at -200C. Bile, obtained from the cannulated common bile duct of lightly ether-anesthetized Sprague-Dawley rats, was centrifuged at 2500 g for 30 min. The clear supernate was passed through a Sephadex G-25 column, equilibrated with SPB, to remove bile acids (13). The protein eluted in the void volume was concentrated by ultrafiltration to 1.5 mg protein/ml.

show abstract

“…(4) Anti-normal liver h protein antiserum Rabbit antiserum directed against purified aminoazo dye-binding h protein from normal Wistar rat liver was the same as that prepared previously (Baldwin et al, 1968).…”

Section: Methodsmentioning

confidence: 99%