scholarly journals The Structure of Surface-Denatured Protein. III. Determination of the Shape of Surface-Denatured Horse Serum Albumin

1952 ◽  
Vol 25 (1) ◽  
pp. 13-16 ◽  
Author(s):  
Kazutomo Imahori
Keyword(s):  
Serum Albumin ◽  
Horse Serum ◽  
Denatured Protein

scholarly journals ANTIGENIC PROPERTIES OF NATIVE AND REGENERATED HORSE SERUM ALBUMIN

1943 ◽  
Vol 78 (1) ◽  
pp. 1-8 ◽  
Author(s):  
John O. Erickson ◽  
Hans Neurath
Keyword(s):  
Serum Albumin ◽  
Protein Denaturation ◽  
Horse Serum ◽  
Native State ◽  
Immunological Activity ◽  
Denatured Protein ◽  
Antigenic Activity ◽  
Antigenic Properties ◽  
The Mean ◽  
Physical And Chemical

Comparative immunological measurements have been carried out on crystalline horse serum albumin in the native state and after regeneration from 8 M urea solutions. The mean antigenic activity of the regenerated protein has been found to be less than 10 per cent of that of the native, whereas both antigens proved to be immunologically equivalent. The problem of the relation between protein denaturation and immunological activity has been considered and discussed on the basis of known physical and chemical differences between native and denatured protein.

scholarly journals ABSENCE OF METHIONINE IN CRYSTALLINE HORSE SERUM ALBUMIN

1941 ◽  
Vol 141 (3) ◽  
pp. 999-1000
Author(s):  
Erwin Brand ◽  
Beatrice Kassell
Keyword(s):  
Serum Albumin ◽  
Horse Serum

scholarly journals Simultaneous Determination of Human Serum Albumin and Low-Molecular-Weight Thiols after Derivatization with Monobromobimane

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3321
Author(s):  
Katarzyna Kurpet ◽  
Rafał Głowacki ◽  
Grażyna Chwatko
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Simultaneous Determination ◽  
Reversed Phase ◽  
Fluorescence Labeling ◽  
Detector Response ◽  
Low Molecular Weight

Biothiols are extremely powerful antioxidants that protect cells against the effects of oxidative stress. They are also considered relevant disease biomarkers, specifically risk factors for cardiovascular disease. In this paper, a new procedure for the simultaneous determination of human serum albumin and low-molecular-weight thiols in plasma is described. The method is based on the pre-column derivatization of analytes with a thiol-specific fluorescence labeling reagent, monobromobimane, followed by separation and quantification through reversed-phase high-performance liquid chromatography with fluorescence detection (excitation, 378 nm; emission, 492 nm). Prior to the derivatization step, the oxidized thiols are converted to their reduced forms by reductive cleavage with sodium borohydride. Linearity in the detector response for total thiols was observed in the following ranges: 1.76–30.0 mg mL−1 for human serum albumin, 0.29–5.0 nmol mL−1 for α-lipoic acid, 1.16–35 nmol mL−1 for glutathione, 9.83–450.0 nmol mL−1 for cysteine, 0.55–40.0 nmol mL−1 for homocysteine, 0.34–50.0 nmol mL−1 for N-acetyl-L-cysteine, and 1.45–45.0 nmol mL−1 for cysteinylglycine. Recovery values of 85.16–119.48% were recorded for all the analytes. The developed method is sensitive, repeatable, and linear within the expected ranges of total thiols. The devised procedure can be applied to plasma samples to monitor biochemical processes in various pathophysiological states.

Comparison of several methods for semiquantitative determination of urinary protein.

1977 ◽  
Vol 23 (5) ◽  
pp. 876-879 ◽  
Author(s):  
W L Gyure
Keyword(s):  
Serum Albumin ◽  
Salt Concentration ◽  
Urine Samples ◽  
Urine Protein ◽  
Sulfosalicylic Acid ◽  
Green Method ◽  
Semiquantitative Determination ◽  
Acid Method ◽  
Bromcresol Green

Abstract Two types of urine protein dipsticks and the sulfosalicylic acid method were compared for their accuracy and specificity, with use of urine samples supplemented with various proteins. Dipsticks yield accurate results when the protein under consideration is restricted to albumin; the sulfosalicylic acid method accurately determines many kinds of proteins in addition to albumin. Detergents affect each of the methods, but changes in salt concentration only affect results by dipstick procedures. Dipsticks, which are based on the protein-error principle for indicators, are subject to some of the conditions that apply to the bromcresol green method for serum albumin determination.

scholarly journals Determination of 1,5‒anhydro‒glucitol–carrier protein conjugates by matrix‒assisted laser desorption/ionization tof mass spectrometry and antibody formation

2000 ◽  
Vol 14 (3) ◽  
pp. 85-92 ◽  
Author(s):  
Li-Jiang Xuan ◽  
Hiroyuki Tanaka ◽  
Satoshi Morimoto ◽  
Yukihiro Shoyama ◽  
Hiroshi Akanuma ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Serum Albumin ◽  
Laser Desorption ◽  
Laser Desorption Ionization ◽  
Protein Conjugates ◽  
Desorption Ionization ◽  
Chicken Lysozyme ◽  
Matrix Assisted Laser ◽  
Matrix Assisted Laser Desorption

In order to prepare the monoclonal antibody against 1,5-anhydro-glucitol (1), it was conjugated with bovine serum albumin (BSA), human serum albumin (HSA) or chicken lysozyme (CL) using succinate orβ-alanine succinate as a spacer to produce individual antigen conjugates. The number of hapten contained in each antigen conjugate was determined by matrix-assisted laser desorption/ionization tof mass (MALDI-tof-MS) spectrometry. The formation of monoclonal antibody (MAb) was also discussed.

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