Hydrated multibilayers of 1-palmitoyl-2-monobromopalmitoyl-sn-glyeero-3-phosphorylcholine (BrDPPC), where the 2-chain is brominated at either the C-9 or C-10 position, have been studied by low and wide angle X-ray diffraction methods. Oriented and unoriented samples were investigated. The long spaci
β¦ LIBER β¦
Bitis gabonica venom: A kinetic analysis of the hydrolysis by phospholipase A2 of 1,2-dipalmitoyl-sn-glycero-3-phosphorylcholine
β Scribed by Cornelis C. Viljoen; Johannes C. Schabort; Dawie P. Botes
- Book ID
- 115736884
- Publisher
- Elsevier Science
- Year
- 1974
- Tongue
- English
- Weight
- 719 KB
- Volume
- 360
- Category
- Article
- ISSN
- 0005-2760
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Structural properties of a monobrominate
β
R.K. Lytz; J.C. Reinert; S.E. Church; H.H. Wickman
π
Article
π
1984
π
Elsevier Science
π
English
β 697 KB
Evidence for O-acyl cleavage during hydr
β
Michael A. Wells
π
Article
π
1971
π
Elsevier Science
π
English
β 551 KB
Spectral properties of Bitis gabonica ve
β
C.C. Viljoen; D.P. Botes; J.C. Schabort
π
Article
π
1975
π
Elsevier Science
π
English
β 511 KB
Influence of pH on the kinetic and spect
β
Cornelis C. Viljoen; Dawie P. Botes
π
Article
π
1979
π
Elsevier Science
π
English
β 606 KB
Hydrolysis of 1-triacontanoyl-2-(pyren-1
β
Tom ThurΓ©n; Jorma A. Virtanen; Petri Vainio; Paavo K.J. Kinnunen
π
Article
π
1983
π
Elsevier Science
π
English
β 422 KB
1-Hexadecyl-2-Arachidonoylthio-2-deoxy-s
β
L.J. Reynolds; L.L. Hughes; L. Yu; E.A. Dennis
π
Article
π
1994
π
Elsevier Science
π
English
β 726 KB
Human cytosolic phospholipase \(\mathbf{A}_{2}\left(\mathrm{cPLA}_{2}\right)\) is an 85kDa protein which displays a preference for arachidonoyl phospholipids as substrates. This substrate preference and the assay characteristics of the enzyme are quite different from those of the smaller, more wells