High-affinity binding of laurate to naturally occurring mutants of human serum albumin and proalbumin.
about
A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties.Oxidation of human serum albumin exhibits inter-individual variability after an ultra-marathon mountain race.Differential effects of xanthine oxidase inhibition and exercise on albumin concentration in rat tissues.Mutations and polymorphisms of the gene of the major human blood protein, serum albumin.
P2860
High-affinity binding of laurate to naturally occurring mutants of human serum albumin and proalbumin.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
High-affinity binding of laura ...... serum albumin and proalbumin.
@en
type
label
High-affinity binding of laura ...... serum albumin and proalbumin.
@en
prefLabel
High-affinity binding of laura ...... serum albumin and proalbumin.
@en
P2093
P2860
P356
P1433
P1476
High-affinity binding of laura ...... serum albumin and proalbumin.
@en
P2093
Brennan SO
Galliano M
Kragh-Hansen U
Minchiotti L
Pedersen AO
Salzano FM
Tárnoky AL
P2860
P304
P356
10.1042/BJ3200911
P407
P478
320 ( Pt 3)
P577
1996-12-01T00:00:00Z