scholarly journals The effect of cardiolipin side chain composition on cytochrome c protein conformation and peroxidase activity

2021 ◽  
Vol 9 (5) ◽  
Author(s):  
Jennifer A. Wilkinson ◽  
Sebastian Silvera ◽  
Paul J. LeBlanc
Keyword(s):  
Cytochrome C ◽  
Peroxidase Activity ◽  
Protein Conformation ◽  
Side Chain ◽  
C Protein ◽  
Chain Composition

Biocompatible fluorinated polyglycerols for droplet microfluidics as an alternative to PEG-based copolymer surfactants

Lab on a Chip ◽  
2016 ◽  
Vol 16 (1) ◽  
pp. 65-69 ◽  
Author(s):  
Olaf Wagner ◽  
Julian Thiele ◽  
Marie Weinhart ◽  
Linas Mazutis ◽  
David A. Weitz ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Encapsulation ◽  
Droplet Microfluidics ◽  
Side Chain ◽  
Expression Studies ◽  
Chain Composition ◽  
Gene Expression Studies

Polyglycerol-based triblock surfactants with tailored side-chain composition are exemplified in cell encapsulation and in vitro gene expression studies in droplet-based microfluidics as alternative to PEG-based surfactants.

scholarly journals Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity

2014 ◽  
Vol 111 (18) ◽  
pp. 6648-6653 ◽  
Author(s):  
L. J. McClelland ◽  
T.-C. Mou ◽  
M. E. Jeakins-Cooley ◽  
S. R. Sprang ◽  
B. E. Bowler
Keyword(s):  
Cytochrome C ◽  
Peroxidase Activity ◽  
Mitochondrial Cytochrome ◽  
Mitochondrial Cytochrome C

The proportion of Met80-sulfoxide dictates peroxidase activity of human cytochrome c

2018 ◽  
Vol 47 (27) ◽  
pp. 9128-9135 ◽  
Author(s):  
Rinky D. Parakra ◽  
Torsten Kleffmann ◽  
Guy N. L. Jameson ◽  
Elizabeth C. Ledgerwood
Keyword(s):  
Cytochrome C ◽  
Peroxidase Activity ◽  
Human Cytochrome ◽  
Human Cytochrome C

Peroxidase activity of cytochrome c is activated and deactivated by methionine 80 oxidation to the sulfoxide and sulfone respectively.

ON THE IDENTITY OF PLATELET FIBRINOGEN WITH PLASMA FIBRINOGEN

1987 ◽  
Author(s):  
H Kaudewitz ◽  
A Henschen ◽  
R E Zimmermann
Keyword(s):  
High Performance ◽  
Reversed Phase ◽  
Plasma Fibrinogen ◽  
Side Chain ◽  
Terminal Sequence ◽  
Hplc Fingerprint ◽  
Amino Terminal ◽  
Chain Composition ◽  
Established Fact ◽  
Amino Terminal Sequence

It is a well established fact that fibrinogen occurs not only in blood plasma but also in the α-granules of the platelets. Recently, it has been shown that fibrinogen is synthesised in the megakaryocytes as well as in the liver. Plasma fibrinogen is derived from the liver, but platelet fibrinogen either exclusively or partially from the megakaryocytes. Conclusive, proteinche-mical evidence for the identity of the fibrinogens from the two biosynthetic sources has previously not been produced. However, the two fibrinogen preparations have been shown to have the same overall peptide chain composition, to be thrombin-clottable and release fibrinopeptides of A- and B-type, and to react with antibodies against plasma fibrinogen. The two preparations differ in the way that platelet fibrinogen lacks the higher-molecular-mass γ-chain variant.The aim of the present investigation was to conduct a detailed proteinchemical comparison between human plasma and platelet fibrinogen. For this purpose, fibrin(ogen)s from the two sources were mercaptolysed, alkylated and the three peptide chains isolated by reversed-phase high-performance liquid chromatography (HPLC). The peptide chains were then analysed directly for amino-terminal sequence and for carboxyterminal sequence by isolation of a terminal fragment. The HPLC-fingerprint patterns of the cyanogen bromide-cleaved chains were compared. The native fibrinogens were also treated with thrombin and the fibrinopeptide type distribution determined by reversed-phase HPLC. The carbohydrate side chain compositions were established by ion-exchange-chromatographic methods after acid hydrolysis. So far no previously unrecognized differences have been observed.

Functional modulation of cytochrome C upon specific binding to DNA nanoribbons

2019 ◽  
Vol 55 (93) ◽  
pp. 14074-14077
Author(s):  
Xiangyuan Ouyang ◽  
Si-Yao Wang ◽  
Ting Liu ◽  
Yong-An Ren ◽  
Mei-Fang Wang ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Peroxidase Activity ◽  
Specific Binding ◽  
Redox Activity ◽  
Functional Modulation

We discovered that the redox activity of cytochrome C can be enhanced and its peroxidase activity can be decreased by DNA nanoribbons.

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