Organ and species specificity of mouse uterine alkaline phosphatase
โ Scribed by Dufour, D. ;Tremblay, A. ;Taskar, S. ;Estrada, R.
- Publisher
- John Wiley and Sons
- Year
- 1972
- Tongue
- English
- Weight
- 617 KB
- Volume
- 179
- Category
- Article
- ISSN
- 0022-104X
No coin nor oath required. For personal study only.
โฆ Synopsis
An alkaline phosphatase was isolated from saline extract of mouse uterus by the method of isoelectric focussing. The organ and species specificity of this protein was demonstrated by immunodiffusion studies. This phosphatase was localized immunohistochemically in the endometrical epithelium of mouse uterus.
๐ SIMILAR VOLUMES
## WITH THE TECHNICAL ASSISTANCE OF N THE preceding paper6 it was shown that I injection of the mitochondria1 fraction of rat lymphosarcoma into rabbits produces relatively high titered antisera reacting with a lipid fraction extractable from the whole tissue with chloroform-methanol. There were t
The tissue and developmental specificities of the acid phosphatase (ACPH) isozymes of Triticum aestivum and its progenitor species T. turgidum and T. tauschii have been determined and compared using the zymogram technique. Tissue and/or developmental variation in relative staining intensity, suggest
Phosphate depleted Pyrocystis noctiluca (Murray) Schuett 1895 has at least one phosphomonoesterase (EC 3:1 : 3:1 ) which is triphasic between 0.1 and 222 pmol P. The enzyme has a broad temperature range with maximum activity at 50 ~ and a Q10 of 1.4 to 1.5. A break in the Arrhenius plot at 35 ~ impl
Faithful and efficient transcription initiation at the mouse ribosomal gene promoter requires besides RNA polymerase I (pol I) four polypeptide trans-acting factors, termed TIF-IA, TIF-IB, TIF-IC, and mUBF. We have partially purified these proteins from cultured Ehrlich ascites cells and show that i