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Binding of uteroglobin to microsomes and plasmatic membranes.
- Source :
-
FEBS letters [FEBS Lett] 1995 Mar 20; Vol. 361 (2-3), pp. 255-8. - Publication Year :
- 1995
-
Abstract
- Microsomes and plasmatic membranes from rat liver bind radioactive uteroglobin (UG) in vitro with high affinity (Kd = 1.7 x 10(-10) M. The binding is saturable and specific and dependent on previous reduction of UG with dithiothreitol. Microsomes from rat spleen or lung or from rabbit endometrium also possess a similar ability. Binding capacity is not affected by previous treatment of microsomes with phospholipase A2 or peptide-N-glycosidase F but is lost after brief treatment with trypsin. The complex formed between UG and the binding component can be solubilized from microsomes with 5 mM CHAPS and it elutes with an apparent Mr of 90,000 in a Sephacryl 200 column. The complex is resistant to 8 M urea but is completely dissociated by Triton X-100. The UG-binding protein(s) has been partially purified from solubilized microsomes and membranes by affinity chromatography. The results are discussed in relation to a possible physiological effect of UG on cellular membranes.
- Subjects :
- Animals
Carrier Proteins isolation & purification
Cholic Acids
Chromatography, Affinity
Chromatography, Gel
Detergents
Electrophoresis, Polyacrylamide Gel
Endometrium metabolism
Female
Intracellular Membranes metabolism
Kinetics
Lung metabolism
Octoxynol pharmacology
Phospholipases A pharmacology
Phospholipases A2
Protein Binding
Rabbits
Rats
Spleen metabolism
Trypsin pharmacology
Urea pharmacology
Carrier Proteins metabolism
Cell Membrane metabolism
Microsomes metabolism
Uteroglobin metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 361
- Issue :
- 2-3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 7698333
- Full Text :
- https://doi.org/10.1016/0014-5793(95)00167-8