In vitro Distribution of Americium in Human Blood Serum Proteins

Nature ◽  
1966 ◽  
Vol 210 (5042) ◽  
pp. 1283-1284 ◽  
Author(s):  
G. BOOCOCK ◽  
D. S. POPPLEWELL
Keyword(s):  
Blood Serum ◽  
Human Blood ◽  
Serum Proteins ◽  
Human Blood Serum ◽  
Blood Serum Proteins

Mechanical properties of adsorption layers in solutions of human blood serum proteins: A comparative assessment

2007 ◽  
Vol 52 (4) ◽  
pp. 510-514 ◽  
Author(s):  
T. A. Yakhno ◽  
V. V. Kazakov ◽  
A. G. Sanin ◽  
O. B. Shaposhnikova ◽  
A. S. Chernov
Keyword(s):  
Mechanical Properties ◽  
Blood Serum ◽  
Human Blood ◽  
Serum Proteins ◽  
Comparative Assessment ◽  
Human Blood Serum ◽  
Blood Serum Proteins ◽  
Adsorption Layers

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 .

scholarly journals Quench me if you can: Alpha-2-macroglobulin trypsin complexes enable serum biomarker analysis by MALDI mass spectrometry

2020 ◽  
Author(s):  
Aleksandr S. Taraskin ◽  
Konstantin K. Semenov ◽  
Aleksandr V. Protasov ◽  
Alexey A. Lozhkov ◽  
Alexandr A. Tyulin ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Blood Serum ◽  
Proteolytic Activity ◽  
Human Blood ◽  
Serum Proteins ◽  
Maldi Mass Spectrometry ◽  
Human Blood Serum ◽  
Serum Biomarker ◽  
Biomarker Analysis

ABSTRACTOne of the main functions of alpha-2-macroglobulin (A2M) in human blood serum is the binding of all classes of protease. It is known that trypsin, after such interaction, possesses modified proteolytic activity. Trypsin first hydrolyzes two bonds in A2M’s ‘bait region’, and the peptide 705VGFYESDVMGR715 is released from A2M. In this work, specifics of the A2M-trypsin interaction were used to determine A2M concentration directly in human blood serum using MALDI mass-spectrometry. Following exogenous addition of trypsin to human blood serum in vitro, the concentration of the VGFYESDVMGR peptide was measured, using its isotopically-labeled analogue (18O), and A2M concentration was calculated. The optimized mass spectrometric approach was verified using a standard method for A2M concentration determination (ELISA) and the relevant statistical analysis methods. It was also shown that trypsin’s modified proteolytic activity in the presence of serum A2M can be used to analyze other serum proteins, including potential biomarkers of pathological processes. Thus, this work describes a promising approach to serum biomarker analysis that can be technically extended in several useful directions.

Influence of liposome charge and composition on their interaction with human blood serum proteins

1993 ◽  
Vol 120 (2) ◽  
pp. 119-126 ◽  
Author(s):  
Trinidad Hern�ndez-Caselles ◽  
Jos� Villala�n ◽  
Juan C. G�mez-Fern�ndez
Keyword(s):  
Blood Serum ◽  
Human Blood ◽  
Serum Proteins ◽  
Human Blood Serum ◽  
Blood Serum Proteins

Differential scanning calorimetry of human blood serum exposed in vitro to X-ray radiation

2019 ◽  
Vol 680 ◽  
pp. 178358 ◽  
Author(s):  
Agnieszka Kiełboń ◽  
Anna Michnik ◽  
Kinga Polaczek Grelik ◽  
Klaudia Duch ◽  
Ewa Sadowska-Krępa
Keyword(s):  
Differential Scanning Calorimetry ◽  
Blood Serum ◽  
Human Blood ◽  
Human Blood Serum ◽  
Scanning Calorimetry ◽  
X Ray

scholarly journals Identification of hepatitis C in human blood serum by near-infrared Raman spectroscopy

2008 ◽  
Vol 22 (5) ◽  
pp. 387-395 ◽  
Author(s):  
Jamil Saade ◽  
Marcos Tadeu Tavares Pacheco ◽  
Maira Regina Rodrigues ◽  
Landulfo Silveira Jr.
Keyword(s):  
Raman Spectroscopy ◽  
Hepatitis C ◽  
Blood Serum ◽  
Human Blood ◽  
Near Infrared ◽  
Viral Infections ◽  
Human Blood Serum ◽  
Biochemical Alterations ◽  
Viral Hepatitis C

Hepatitis C has become one of the higher health problems around the world. Near-infrared Raman spectroscopy had been used to spectrally differentiate among health human blood serum from the one with hepatitis C contaminationin vitro. In this study a Raman spectrometer with 80 mW, 830 nm excitation, liquid-nitrogen cooled CCD and imaging spectrograph were used to collect Raman scattering from 24 blood samples (14 healthy and 10 diseased) with collection time of 120 s. It has been used an algorithm based on the Principal Components Analysis (PCA) for main spectral features identification and Mahalanobis distance for blood spectrum classification depending on the serology. It was observed that the highest spectral differences between the two types of human blood serum were found in 1002, 1169, 1262 and 1348 cm−1Raman bands. The spectral analysis using multivariate statistics presented good results when compared to classical diagnosis for viral hepatitis C, showing that Raman spectroscopy can classify human blood serum spectrum in one of the two categories by identifying biochemical alterations that occur in the presence of viral infections.

LIFE IN ZERO MAGNETIC FIELD. III. EFFECT ON ZINC AND COPPER IN HUMAN BLOOD SERUM DURING IN VITRO AGING

2001 ◽  
Vol 20 (2) ◽  
pp. 127-139 ◽  
Author(s):  
Lorelai I. Ciortea ◽  
V. V. Morariu ◽  
Alina Todoran ◽  
S. Popescu
Keyword(s):  
Magnetic Field ◽  
Blood Serum ◽  
Human Blood ◽  
Human Blood Serum ◽  
Zero Magnetic Field ◽  
In Vitro Aging
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