A procedure for the isolation of enzymically active rat-liver nuclei

Widnell, C.C.; Tata, Jamshed R.

doi:10.1042/bj0920313

Cited by 552 publications

(152 citation statements)

References 21 publications

Supporting

Mentioning

142

Contrasting

Unclassified

Order By: Relevance

“…A number of points argue against the possibility of signific~t contamination of the nuclei with non-nuclear LH-RH binding material. The nuclei were prepared by methodology previously shown to produce a purified preparation [9][10][11]18,19] and bound LH-RH with a substantial capacity. The purity of these nuclei was established by electron microscopic examinations.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Luteinizing hormone‐releasing hormone (LH‐RH) binding to purified rat pituitary nuclei

et al. 1983

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

“…The supernatant was centrifuged at 20000 x g for 20 min to give a crude membrane preparation [ 171. Purified nuclei were prepared by a method modified from [18,19]. The crude nuclear pellet was resuspended in a 2.3 M sucrose, 15 mM Tris-HCl, 25 mM KCl, 1.5 mM MgCl2 (pH 7.5) and centrifuged at 18000 x g for 10 min.…”

Section: Preparation Of Nucleimentioning

confidence: 99%

Luteinizing hormone‐releasing hormone (LH‐RH) binding to purified rat pituitary nuclei

et al. 1983

View full text Add to dashboard Cite

show abstract

“…Polyacrylamide gel electrophoresis (PAGE) was performed by a previously described modification of the Laemmli method (6), and Western blotting was done as described by Towbin et al(l1). Rat liver nuclei were prepared by the method of Widnell and Tata (12), and the initial supernatant was used as the cytoplasmic fraction. Protein was measured by the Bio-Rad protein assay (13).…”

Section: Methodsmentioning

confidence: 99%

The association between Mi‐2 antibodies and dermatomyositis

Targoff¹,

Reichlin²

1985

Arthritis & Rheumatism

240

128

View full text Add to dashboard Cite

Antibodies to Mi, an antigen in calf thymus extract, have been demonstrated by complement fixation inhibition in polymyositis (PM) and dermatomyositis (DM) sera but not in the sera of individuals without myositis. The original Mi reference serum defined 2 precipitating antibodies, using immunodiffusion (ID). Anti‐Mi‐1 was not active in complement fixation. We have now studied in further detail anti‐Mi‐2, which appears to be the antibody in Mi serum that fixes complement. Mi‐2 antigen was purified by immunoaffinity chromotography. An enzyme‐linked immunosorbent assay (ELISA) to measure Mi‐2 antibody, using this antigen, was used to test the sera of 139 myositis patients: 52 had DM and 87 had PM. Control sera from 35 normal subjects and 93 patients with other connective tissue diseases were also tested. Only 13 sera were considered definitely positive for anti‐Mi‐2. All were from patients who had myositis, 11 of whom had DM. Only DM sera had anti‐Mi‐2 by ID, and all sera with anti‐Mi‐2 by ID were positive by ELISA. A number of other sera, including many from patients with other connective tissue diseases and 2 from normal subjects (all without precipitating antibodies) had lower elevations which were of uncertain significance. Detection of anti‐Mi‐2 by ID as well as by ELISA was significantly more frequent in DM than in PM. Anti‐Mi‐2 appears to be closely linked to DM, and is the first specific serologic marker for this form of myositis.

show abstract

“…In addition, the subcellular distribution of uterine peroxidase and its induction by physiological amounts of oestrogen is reported. Vol (Widnell & Tata, 1964 [4-'4C]oestradiol (1.84UMM), 2,4-dichlorophenol (0.25 mM), H202 (0.25 mM) and bovine serum albumin (0mg) in 0.1 M-sodium phosphate buffer, pH7.4; total volume 4ml. After incubation, the medium was extracted three times with equal volumes of peroxidefree ether and the combined organic phase was dried over anhydrous Na2SO4.…”

mentioning

confidence: 99%

Metabolism of [4-14C]oestradiol by oestrogen-induced uterine peroxidase

Lyttle

Jellinck

1972

Biochemical Journal

View full text Add to dashboard Cite

1. An enzyme that catalyses the metabolism and binding of [4-14C]oestradiol to protein and to other high-molecular-weight substances in the presence of H2O2 was shown to be absent from the uteri of immature rats and to be induced by physiological doses of oestrogen or pregnant-mare-serum gonadotrophin. 2. The pH optimum, stability to heat and other characteristics of the uterine enzyme system as well as its subcellular distribution were determined. 3. The increase in the ability of uterine preparations to convert [4-14C]oestradiol into water-soluble products as a result of oestrogen treatment was accompanied by an increase in peroxidase and NADH oxidase activities and was inhibited by actinomycin D and cycloheximide. 4. The results support the proposal that the increase in peroxidase activity after oestrogen treatment might be part of an adaptive response of the uterus permitting it to bind and inactivate oestrogens and thus limit the duration of their effect upon this target tissue.

show abstract

A procedure for the isolation of enzymically active rat-liver nuclei

Cited by 552 publications

References 21 publications

Luteinizing hormone‐releasing hormone (LH‐RH) binding to purified rat pituitary nuclei

Luteinizing hormone‐releasing hormone (LH‐RH) binding to purified rat pituitary nuclei

The association between Mi‐2 antibodies and dermatomyositis

Metabolism of [4-14C]oestradiol by oestrogen-induced uterine peroxidase

Contact Info

Product

Resources

About