Effect of low molecular weight human serum factors and human somatomedin peptides on human lymphocyte cultures

1982 ◽  
Vol 57 (1) ◽  
pp. 129-137
Author(s):  
MH Heulin ◽  
M Artur ◽  
J Straczek ◽  
F Belleville ◽  
P Nabet ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
Human Lymphocyte ◽  
Low Molecular Weight ◽  
Serum Factors ◽  
Lymphocyte Cultures

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.

Anti-Inflammatory Activity in the Low Molecular Weight Fraction of Commercial Human Serum Albumin (LMWF5A)

2015 ◽  
Vol 37 (1) ◽  
pp. 55-67 ◽  
Author(s):  
Gregory W. Thomas ◽  
Leonard T. Rael ◽  
Charles W. Mains ◽  
Denetta Slone ◽  
Matthew M. Carrick ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Weight Fraction ◽  
Inflammatory Activity ◽  
Low Molecular Weight ◽  
Anti Inflammatory

State of iron(III) in normal human serum: low molecular weight and protein ligands besides transferrin

1970 ◽  
Vol 48 (12) ◽  
pp. 1339-1350 ◽  
Author(s):  
Bibudhendra Sarkar
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
Binding Capacity ◽  
Normal Serum ◽  
Normal Human Serum ◽  
Void Volume ◽  
Antibody Concentration ◽  
Low Molecular Weight ◽  
Protein Ligands ◽  
Normal Human

A fraction of Fe(III) in normal human serum is bound to both low molecular weight as well as protein ligands besides transferrin. Citrate was shown to be the major Fe(III)-binding substance in the low molecular weight fraction. Amino acids, sugars, and organic acids, such as ascorbate, pyruvate, and lactate, showed very little or no binding to Fe(III) in normal serum. Iron(III)-binding proteins other than transferrin were shown to be present in normal serum when the native serum with [59Fe(III)] was fractionated by (NH4)2SO4 and Sephadex G-150. The presence of these proteins was observed when trace amounts of Fe(III) were added to the normal serum and when the iron-binding capacity was saturated with Fe(III) to 50% and 100%. These proteins were eluted in the void volume of Sephadex G-150 and none of them corresponded electrophoretically to transferrin. The results of the gel filtration of a mixture of [131I]-transferrin and the proteins eluted in the void volume of Sephadex G-150 were strongly in favor of the Fe(III)-proteins as being neither transferrin aggregates nor transferrin adducts with other proteins. Immunoelectrophoresis of the Sephadex G-150 void volume proteins on agar gel against the antibody to transferrin revealed the absence of transferrin. The presence of at least six proteins in this fraction was shown by immunoelectrophoresis. Positive precipitin reactions were obtained with the antibodies to α2-macroglobulin, γG-globulin, γA-globulin, and γM-globulin. At least two more proteins in this fraction remained unidentified. When the same fraction containing [59Fe(III)] was treated with the whole antisera and the precipitates were counted for radioactivity, a typical antigen-antibody reaction curve was obtained as the antibody concentration was increased. Similar experiments with this fraction and antibodies to α2-macroglobulin, γG-globulin, γA-globulin, and γM-globulin failed to show any significant radioactivity in the precipitate. Since this fraction did not contain any transferrin, it was concluded that there are proteins besides transferrin which can act as ligands for Fe(III) in normal blood plasma.

Low-molecular-weight human serum proteome using ultrafiltration, isoelectric focusing, and mass spectrometry

2004 ◽  
Vol 25 (9) ◽  
pp. 1299-1306 ◽  
Author(s):  
Robert G. Harper ◽  
Sarah R. Workman ◽  
Shayne Schuetzner ◽  
Aaron T. Timperman ◽  
Jennifer N. Sutton
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Human Serum ◽  
Isoelectric Focusing ◽  
Low Molecular Weight ◽  
Serum Proteome

Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF

1982 ◽  
Vol 108 (4) ◽  
pp. 1581-1587 ◽  
Author(s):  
James F. Lenney ◽  
John Rose Liao ◽  
Sonia L. Sugg ◽  
Vijaya Gopalakrishnan ◽  
Henry C.H. Wong ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Synovial Fluid ◽  
Human Serum ◽  
Low Molecular Weight

A heat stable low molecular weight inhibitor of lysosomal cysteine proteinases in human serum

1983 ◽  
Vol 110 (2) ◽  
pp. 449-455 ◽  
Author(s):  
Francis Gauthier ◽  
Maurice Pagano ◽  
Frédéric Esnard ◽  
Henri Mouray ◽  
Robert Engler
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
Low Molecular Weight ◽  
Cysteine Proteinases ◽  
Heat Stable
Sign in / Sign up

Export Citation Format

Share Document