Optimized protocol for soluble prokaryotic expression, purification and refolding of the human inhibin α subunit, a cysteine rich peptide chain

2020 ◽  
Vol 28 (2) ◽  
pp. 131-139 ◽  
Author(s):  
Sedighe Kolivand ◽  
Mahboobeh Nazari ◽  
Mohammad Hossein Modarressi ◽  
Mohammad Reza Hosseini Najafabadi ◽  
Atefeh Hemati ◽  
...  
Keyword(s):  
Prokaryotic Expression ◽  
Peptide Chain ◽  
Α Subunit ◽  
Subunit A ◽  
Optimized Protocol

scholarly journals Phylogenomic Analyses Reveal the Evolutionary Origin of the Inhibin α-Subunit, a Unique TGFβ Superfamily Antagonist

PLoS ONE ◽  
2010 ◽  
Vol 5 (3) ◽  
pp. e9457 ◽  
Author(s):  
Jie Zhu ◽  
Edward L. Braun ◽  
Satomi Kohno ◽  
Monica Antenos ◽  
Eugene Y. Xu ◽  
...  
Keyword(s):  
Evolutionary Origin ◽  
Α Subunit ◽  
Subunit A ◽  
Phylogenomic Analyses ◽  
Tgfβ Superfamily

scholarly journals Isolation and Characterization of Anaerobic Ethylbenzene Dehydrogenase, a Novel Mo-Fe-S Enzyme

2001 ◽  
Vol 183 (15) ◽  
pp. 4536-4542 ◽  
Author(s):  
Hope A. Johnson ◽  
Dale A. Pelletier ◽  
Alfred M. Spormann
Keyword(s):  
Amino Acid ◽  
Α Subunit ◽  
Subunit A ◽  
Binding Domains ◽  
Isolation And Characterization ◽  
Apparent Homogeneity ◽  
Dimethyl Sulfoxide Reductase ◽  
Encoding Genes ◽  
Acid Labile

ABSTRACT The first step in anaerobic ethylbenzene mineralization in denitrifying Azoarcus sp. strain EB1 is the oxidation of ethylbenzene to (S)-(−)-1-phenylethanol. Ethylbenzene dehydrogenase, which catalyzes this reaction, is a unique enzyme in that it mediates the stereoselective hydroxylation of an aromatic hydrocarbon in the absence of molecular oxygen. We purified ethylbenzene dehydrogenase to apparent homogeneity and showed that the enzyme is a heterotrimer (αβγ) with subunit masses of 100 kDa (α), 35 kDa (β), and 25 kDa (γ). Purified ethylbenzene dehydrogenase contains approximately 0.5 mol of molybdenum, 16 mol of iron, and 15 mol of acid-labile sulfur per mol of holoenzyme, as well as a molydopterin cofactor. In addition to ethylbenzene, purified ethylbenzene dehydrogenase was found to oxidize 4-fluoro-ethylbenzene and the nonaromatic hydrocarbons 3-methyl-2-pentene and ethylidenecyclohexane. Sequencing of the encoding genes revealed thatebdA encodes the α subunit, a 974-amino-acid polypeptide containing a molybdopterin-binding domain. The ebdB gene encodes the β subunit, a 352-amino-acid polypeptide with several 4Fe-4S binding domains. The ebdC gene encodes the γ subunit, a 214-amino-acid polypeptide that is a potential membrane anchor subunit. Sequence analysis and biochemical data suggest that ethylbenzene dehydrogenase is a novel member of the dimethyl sulfoxide reductase family of molybdopterin-containing enzymes.

The Heterogeneity of Porcine 32,000 MrInhibin α-Subunit: A Gel Electrophoresis and Immunoblot Study*

Endocrinology ◽  
1990 ◽  
Vol 127 (3) ◽  
pp. 1477-1486 ◽  
Author(s):  
KATHERINE H. MOORE ◽  
BONNIE S. DUNBAR ◽  
GEORGE R. BOUSFIELD ◽  
DARRELL N. WARD
Keyword(s):  
Gel Electrophoresis ◽  
Α Subunit ◽  
Subunit A

scholarly journals Optimized protocol for soluble prokaryotic expression, purification and structural analysis of human placenta specific-1(PLAC1)

2017 ◽  
Vol 133 ◽  
pp. 139-151 ◽  
Author(s):  
Mahboobeh Nazari ◽  
Amir-hassan Zarnani ◽  
Roya Ghods ◽  
Rahman Emamzadeh ◽  
Somayeh Najafzadeh ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Human Placenta ◽  
Prokaryotic Expression ◽  
Optimized Protocol
Sign in / Sign up

Export Citation Format

Share Document