Hydrophobic Probe Binding of β-Lactoglobulin in the Native and Molten Globule State Induced by High Pressure as Affected by pH, KIO3andN-Ethylmaleimide

2002 ◽  
Vol 50 (18) ◽  
pp. 5207-5214 ◽  
Author(s):  
Jian Yang ◽  
Joseph R. Powers ◽  
Stephanie Clark ◽  
A. Keith Dunker ◽  
Barry G. Swanson
2001 ◽  
Vol 49 (7) ◽  
pp. 3236-3243 ◽  
Author(s):  
Jian Yang ◽  
A. Keith Dunker ◽  
Joseph R. Powers ◽  
Stephanie Clark ◽  
Barry G. Swanson

Author(s):  
Masamichi Ikeguchi ◽  
Shin-ichi Kato ◽  
Akio Shimizu ◽  
Shintaro Sugai

2010 ◽  
Vol 119 (4) ◽  
pp. 1550-1556 ◽  
Author(s):  
Laurette Tavel ◽  
Céline Moreau ◽  
Saïd Bouhallab ◽  
Eunice C.Y. Li-Chan ◽  
Elisabeth Guichard

Biochemistry ◽  
1999 ◽  
Vol 38 (14) ◽  
pp. 4455-4463 ◽  
Author(s):  
Kazuo Fujiwara ◽  
Munehito Arai ◽  
Akio Shimizu ◽  
Masamichi Ikeguchi ◽  
Kunihiro Kuwajima ◽  
...  

Biochemistry ◽  
2006 ◽  
Vol 45 (51) ◽  
pp. 15468-15473 ◽  
Author(s):  
Kanako Nakagawa ◽  
Akihito Tokushima ◽  
Kazuo Fujiwara ◽  
Masamichi Ikeguchi

1997 ◽  
Vol 44 (4) ◽  
pp. 645-657 ◽  
Author(s):  
R Kuciel ◽  
A Mazurkiewicz

Human prostatic acid phosphatase (hPAP, EC.3.1.3.2), a secretory homodimeric protein was denatured in 6 M urea, pH 2.5, and refolded by dilution at pH 7.2 with recovery of the enzymatic activity and dimeric structure. Circular dichroism, intrinsic fluorescence and chromatographic analysis of renaturating protein suggested that the kinetic intermediate of the hPAP folding is a monomer which displays a molten globule state (R. Kuciel, A. Mazurkiewicz & W.S. Ostrowski, 1996, Int. J. Biol. Macromol. 18, 167-175). To confirm these data experiments were performed to estimate the interaction of the renaturating protein with dyes and amphipathic lipid structures. Increased binding of the hydrophobic probe 1-anilinonaphthalene-8-sulfonate and Congo Red to the refolding enzyme supported the existence of molten globule state with the relaxed beta-structure in the renaturating protein. Presence of liposomes, included in the renaturation mixture as a model of acid phospholipid, resulted in perturbations of the human PAP refolding process. Some folding intermediates were bound to phosphatidylserine liposomes or, alternatively, water soluble, inactive aggregates were formed.


Biochemistry ◽  
1993 ◽  
Vol 32 (48) ◽  
pp. 13198-13203 ◽  
Author(s):  
Akio Shimizu ◽  
Masamichi Ikeguchi ◽  
Shintaro Sugai

1996 ◽  
Vol 257 (4) ◽  
pp. 877-885 ◽  
Author(s):  
Christian Rischel ◽  
Per Thyberg ◽  
Rudolf Rigler ◽  
Flemming M. Poulsen

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