THE CONSTRUCTION OF AN ULTRAFILTRATION UNIT TO MEASURE THE BINDING OF CERTAIN NITROGEN MUSTARDS TO SERUM PROTEIN

1962 ◽  
Vol 40 (1) ◽  
pp. 137-146 ◽  
Author(s):  
J. H. Linford ◽  
J. Legal ◽  
E. Zacharias
Keyword(s):  
Blood Serum ◽  
Cellulose Acetate ◽  
Serum Protein ◽  
Human Blood ◽  
Human Blood Serum ◽  
Cellulose Acetate Membrane ◽  
Nitrogen Mustards ◽  
Benzene Rings ◽  
High Degree

An ultrafiltration unit has been designed, and constructed to contain a 10-ml volume. The unit is leakproof, is self-contained, and can be operated inside a small refrigerator or oven. It has been used with "Visking" cellulose acetate membrane to separate the colloidal protein phase of human blood serum from the aqueous dispersing phase, and to study the distribution of certain nitrogen mustards between these phases. The results indicate that these drugs are adsorbed to the protein to a high degree and that the presence of the benzene rings in the nitrogen mustards is mainly responsible for this adsorption.

THE CONSTRUCTION OF AN ULTRAFILTRATION UNIT TO MEASURE THE BINDING OF CERTAIN NITROGEN MUSTARDS TO SERUM PROTEIN

1962 ◽  
Vol 40 (1) ◽  
pp. 137-146 ◽  
Author(s):  
J. H. Linford ◽  
J. Legal ◽  
E. Zacharias
Keyword(s):  
Blood Serum ◽  
Cellulose Acetate ◽  
Serum Protein ◽  
Human Blood ◽  
Human Blood Serum ◽  
Cellulose Acetate Membrane ◽  
Nitrogen Mustards ◽  
Benzene Rings ◽  
High Degree

An ultrafiltration unit has been designed, and constructed to contain a 10-ml volume. The unit is leakproof, is self-contained, and can be operated inside a small refrigerator or oven. It has been used with "Visking" cellulose acetate membrane to separate the colloidal protein phase of human blood serum from the aqueous dispersing phase, and to study the distribution of certain nitrogen mustards between these phases. The results indicate that these drugs are adsorbed to the protein to a high degree and that the presence of the benzene rings in the nitrogen mustards is mainly responsible for this adsorption.

Notizen: Quantification and Localisation of SH-Groups in Human Blood Serum Proteins

1978 ◽  
Vol 33 (9-10) ◽  
pp. 803-805 ◽  
Author(s):  
E. Schauenstein ◽  
F. Dachs
Keyword(s):  
Blood Serum ◽  
Serum Protein ◽  
Human Blood ◽  
Serum Proteins ◽  
Total Activity ◽  
Expected Value ◽  
Human Blood Serum ◽  
Thiol Groups ◽  
Disulfide Exchange ◽  
Blood Serum Proteins

Abstract The thiol groups of human blood serum proteins were determined after 24 hours interaction with dithionitrobenzoicacid (DTNB) to an average of 538 ± 60 µmol/l serum. After treatment of the serum with [35S]DTNB , autoradiograms of the protein elpherograms revealed two main peaks: The first with 63% of total activity, in the albumin region, corresponding to 0.60 SH/mol, the second with 23% of total activity, in the 7-globulin range, corresponding to 2.2 SH/mol. After 30 minutes incubation with D TNB , or with p-chloromercuribenzoate (CMB), in freshly prepared pools of IgG only 0.2 SH/mol were found which is the expected value already known from the literature.Autoradiograms taken from serum protein elpherograms after interaction with [UC] CMB only show the main SH-peak in the albumin range. Thus ist is concluded that the SH-peak in the γ-globulin region after 24 hours incubation with [35S]DTNB is due to one highly labile S-S-bond which easily undergoes a disulfide exchange with DTNB .

Human Blood Serum Rich in Factor V

1970 ◽  
Vol 24 (03/04) ◽  
pp. 334-337 ◽  
Author(s):  
R Honorato
Keyword(s):  
Blood Serum ◽  
Human Serum ◽  
Human Blood ◽  
Human Blood Serum ◽  
Factor V ◽  
The Stability

Summary1. A technique to obtain human serum rich in factor V is described.2. Calcium increases the stability of factor V in the serum.

scholarly journals THE ELECTRODIALYSIS OF HUMAN BLOOD SERUM

1926 ◽  
Vol 69 (1) ◽  
pp. 113-124
Author(s):  
Adolph Bernhard ◽  
Jacob J. Beaver
Keyword(s):  
Blood Serum ◽  
Human Blood ◽  
Human Blood Serum

scholarly journals Tagetes erecta as an organic precursor: synthesis of highly fluorescent CQDs for the micromolar tracing of ferric ions in human blood serum

RSC Advances ◽  
2021 ◽  
Vol 11 (32) ◽  
pp. 19924-19934
Author(s):  
Pinky Sagar ◽  
Gopal Krishna Gupta ◽  
Monika Srivastava ◽  
Amit Srivastava ◽  
S. K. Srivastava
Keyword(s):  
Blood Serum ◽  
Hydrothermal Method ◽  
Human Blood ◽  
Human Blood Serum ◽  
Tagetes Erecta ◽  
Ferric Ions ◽  
Organic Precursor ◽  
Precursor Synthesis

TE-CQDs synthesized via the hydrothermal method for the detection of Fe3+ in HBS.

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