Production and purification of N-terminal half-transferrin in Pichia pastoris.
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Transferrin-mediated cellular iron deliveryCrystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for ironStructural and functional characterization of recombinant human serum transferrin secreted from Pichia pastoris.Properties of a homogeneous C-lobe prepared by introduction of a TEV cleavage site between the lobes of human transferrin.High-yield production of functionally active human serum transferrin using a baculovirus expression system, and its structural characterization.Expression, purification, and partial in vitro characterization of biologically active human coagulation factor VIII light chain (A3-C1-C2) in Pichia pastoris.Overview of protein expression in Pichia pastoris.
P2860
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P2860
Production and purification of N-terminal half-transferrin in Pichia pastoris.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Production and purification of N-terminal half-transferrin in Pichia pastoris.
@en
Production and purification of N-terminal half-transferrin in Pichia pastoris.
@nl
type
label
Production and purification of N-terminal half-transferrin in Pichia pastoris.
@en
Production and purification of N-terminal half-transferrin in Pichia pastoris.
@nl
prefLabel
Production and purification of N-terminal half-transferrin in Pichia pastoris.
@en
Production and purification of N-terminal half-transferrin in Pichia pastoris.
@nl
P356
P1476
Production and purification of N-terminal half-transferrin in Pichia pastoris
@en
P2093
Steinlein LM
P304
P356
10.1006/PREP.1995.1081
P577
1995-10-01T00:00:00Z