Isolation of two 67 kDa calcium-binding proteins from pig lung differing in affinity for phospholipids and in anti-phospholipase A2 activity.
about
Annexin 5 as a potential regulator of annexin 1 phosphorylation by protein kinase C. In vitro inhibition compared with quantitative data on annexin distribution in human endothelial cells.Identification, characterization and purification to near-homogeneity of a novel 67 kDa phosphotyrosyl protein phosphatase associated with pig lung annexin extract.67 k calcimedin (67 kDa) is distinct from p67 calelectrin and lymphocyte 68 kDa Ca2+-binding protein.Activated protein kinase C alpha associates with annexin VI from skeletal muscle.Influence of fibroblast growth factor on phosphorylation and activity of a 34 kDa lipocortin-like protein in bovine epithelial lens cells.
P2860
Isolation of two 67 kDa calcium-binding proteins from pig lung differing in affinity for phospholipids and in anti-phospholipase A2 activity.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Isolation of two 67 kDa calciu ...... nti-phospholipase A2 activity.
@en
type
label
Isolation of two 67 kDa calciu ...... nti-phospholipase A2 activity.
@en
prefLabel
Isolation of two 67 kDa calciu ...... nti-phospholipase A2 activity.
@en
P2093
P2860
P1433
P1476
Isolation of two 67 kDa calciu ...... nti-phospholipase A2 activity.
@en
P2093
I Vilgrain
J Ragab-Thomas
L Douste-Blazy
P2860
P304
P356
10.1016/0014-5793(87)80963-8
P407
P577
1987-09-01T00:00:00Z