Site-specific water proton relaxation enhancement of iron (III) chelates noncovalently bound to human serum albumin

1991 ◽  
Vol 17 (1) ◽  
pp. 164-178 ◽  
Author(s):  
Bruce G. Jenkins ◽  
Eileen Armstrong ◽  
Randall B. Lauffer
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Water Proton ◽  
Proton Relaxation ◽  
Site Specific ◽  
Proton Relaxation Enhancement

Water Proton Relaxation Rate Enhancements and Association Constants for Mn(II) to Serum Proteins Determined by NMR T1 Measurements

2005 ◽  
Vol 60 (9-10) ◽  
pp. 807-812 ◽  
Author(s):  
Hatice Budak
Keyword(s):  
Serum Albumin ◽  
Human Serum ◽  
Relaxation Rate ◽  
Association Constant ◽  
Serum Proteins ◽  
Association Constants ◽  
Water Proton ◽  
Proton Relaxation ◽  
Rate Enhancement ◽  
Human Serum Proteins

Abstract The water proton relaxation rate enhancement of Mn(II) bound to bovine serum albumin (BSA) and the association constant for manganese to BSA have already been determined, but such determinations have not been done for human serum albumin (HSA) and other human serum proteins and also for human serum. In this work, NMR T1 values in aqueous solutions of serum proteins and serum were measured versus increasing concentration of Mn(II). Proton relaxation rate enhancements (ε*) caused by different manganese concentrations were determined for each solution and 1/ε* was fitted against concentrations of Mn(II). Proton relaxation rate enhancements (εb) of Mn(II) bound to albumin, γ-globulin, (α+β)- globulins and serum were found to be 13.69, 3.09, 8.62, and 10.87, respectively. Free and bound manganese fractions, resulted from each addition of Mn(II) to the sample, were determined by using corresponding (ε*) and the εb values. Association constants for Mn(II) to HSA and γ-globulin were calculated as 1.84 x 104 ᴍ-1 and 2.35 x 104 ᴍ-1, respectively. Present data suggest that the proton relaxation rate enhancement of Mn(II) in serum is caused by Mn(II) bound to various serum constituents. Data also suggest that association constants for Mn(II) to γ-globulin are nearly the same as that to HSA.

Site-specific N-terminal Auto-degradation of Human Serum Albumin

1995 ◽  
Vol 227 (1-2) ◽  
pp. 524-528 ◽  
Author(s):  
Bernard Chan ◽  
Neil Dodsworth ◽  
John Woodrow ◽  
Alan Tucker ◽  
Roy Harris
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Site Specific

Comparative studies of the serum half-life extension of a protein via site-specific conjugation to a species-matched or -mismatched albumin

2018 ◽  
Vol 6 (8) ◽  
pp. 2092-2100 ◽  
Author(s):  
Byungseop Yang ◽  
Jong Chul Kim ◽  
Jihyoun Seong ◽  
Giyoong Tae ◽  
Inchan Kwon
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Comparative Studies ◽  
Half Life ◽  
Therapeutic Proteins ◽  
Life Extension ◽  
Site Specific

Human serum albumin (HSA) has been investigated as a serum half-life extender of therapeutic proteins thanks to its unusually long serum half-life.

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