Isolation, characterization and metal-ion-binding properties of the alpha-subunit from S-100a protein.
about
Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution.The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunitsSpectral [corrected] studies on the cadmium-ion-binding properties of bovine brain S-100b protein.Purification and spectral studies on the Ca2+-binding properties of 67 kDa calcimedin.Spectroscopic studies on Tb3+ binding to S-100a protein.Fluorescence studies on the Ca2+ and Zn2+ binding properties of the alpha-subunit of bovine brain S-100a protein.
P2860
Isolation, characterization and metal-ion-binding properties of the alpha-subunit from S-100a protein.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Isolation, characterization an ...... a-subunit from S-100a protein.
@en
type
label
Isolation, characterization an ...... a-subunit from S-100a protein.
@en
prefLabel
Isolation, characterization an ...... a-subunit from S-100a protein.
@en
P2093
P2860
P356
P1433
P1476
Isolation, characterization an ...... a-subunit from S-100a protein.
@en
P2093
P2860
P304
P356
10.1042/BJ2370757
P407
P577
1986-08-01T00:00:00Z