Serum Protein Analysis of Nurse Sharks

2020 ◽  
Vol 32 (2) ◽  
pp. 77-82 ◽  
Author(s):  
Leila AtallahBenson ◽  
Liza Merly ◽  
Carolyn Cray ◽  
Neil Hammerschlag
Keyword(s):  
Serum Protein ◽  
Protein Analysis ◽  
Nurse Sharks

Serum Protein Analysis by Electrophoresis and by the Wolfson-Cohn Chemical Method

1956 ◽  
Vol 2 (5) ◽  
pp. 334-346 ◽  
Author(s):  
Nils Eriksen ◽  
Lester D Ellerbrook ◽  
Stuart W Lippincott
Keyword(s):  
Serum Protein ◽  
Chemical Method ◽  
Electrophoretic Pattern ◽  
Protein Analysis ◽  
Chemical Fractionation ◽  
Major Protein ◽  
Dialysis Membrane ◽  
Percentage Basis ◽  
Source Of Error

Abstract One hundred serum specimens from healthy and diseased adults were analyzed for the major protein constituents by free electrophoresis and by the Wolfson-Cohn chemical method. Albumin values obtained by the two methods were well correlated and were also in good average numerical agreement. The γ-globulin values were well correlated, but were not in quite such good numerical agreement, on a percentage basis, as were the albumin values. The α-globulin values were poorly correlated, as were also the β-globulin values. Electrophoretic examination of some of the chemical fractions indicated that part of the discrepancy between the two methods was caused by faulty chemical fractionation, particularly with respect to the globulin fractions. Determination of total solids retained by a dialysis membrane (TS) in 22 serum specimens confirmed the proportionality between TS and the electrophoretic-pattern area, and emphasized a source of error of undetermined magnitude in the calculation of electrophoretic results from simple protein totals.

Evaluation of two automated capillary electrophoresis systems for human serum protein analysis

2011 ◽  
Vol 44 (17-18) ◽  
pp. 1473-1479 ◽  
Author(s):  
Céline Chartier ◽  
Anne Marie Boularan ◽  
Anne Marie Dupuy ◽  
Stéphanie Badiou ◽  
Anne Sophie Bargnoux ◽  
...  
Keyword(s):  
Capillary Electrophoresis ◽  
Human Serum ◽  
Serum Protein ◽  
Protein Analysis ◽  
Human Serum Protein

scholarly journals Optimization of Utilization of Serum Protein Analysis

2013 ◽  
Vol 139 (6) ◽  
pp. 793-797 ◽  
Author(s):  
Hamid M. Zia ◽  
Gurmukh Singh
Keyword(s):  
Serum Protein ◽  
Protein Analysis

Demonstration of monoclonal IgE by isoelectric focusing: first reported case of IgE myeloma in Australia.

1988 ◽  
Vol 34 (10) ◽  
pp. 2168-2171 ◽  
Author(s):  
R McLachlan ◽  
A P Grigg ◽  
F N Cornell ◽  
R A Harris ◽  
R K Woodruff
Keyword(s):  
Multiple Myeloma ◽  
Back Pain ◽  
Serum Protein ◽  
Isoelectric Focusing ◽  
Protein Analysis ◽  
Monoclonal Immunoglobulins ◽  
Ige Myeloma

Abstract A 56-year-old man who presented with back pain was diagnosed with multiple myeloma. Serum protein analysis by isoelectric focusing identified a monoclonal IgE lambda of unique spectrotype compared with other monoclonal immunoglobulins. The similarity of the spectrotype of this monoclonal IgE to that of two purified monoclonal IgEs suggests that these proteins have a characteristic spectrotype, sufficiently different from those of other immunoglobulin classes to allow its recognition.

Serum protein analysis on immobilized pH gradients within situ adsorption of albumin on Dextran Blue

1985 ◽  
Vol 6 (7) ◽  
pp. 326-331 ◽  
Author(s):  
Elisabetta Gianazza ◽  
Patrizia Giacon ◽  
Silvia Astrua-Testori ◽  
Pier Giorgio Righetti
Keyword(s):  
Serum Protein ◽  
Protein Analysis ◽  
Ph Gradients

Ontogenetic changes in hemoglobin synthesis of two strains of Chironomus tentans

Development ◽  
1969 ◽  
Vol 22 (3) ◽  
pp. 465-476
Author(s):  
Darrel S. English
Keyword(s):  
Molecular Weight ◽  
Serum Protein ◽  
Human Blood ◽  
Protein Analysis ◽  
Chironomus Tentans ◽  
Ontogenetic Changes ◽  
Hemoglobin Synthesis ◽  
Chironomus Plumosus ◽  
Monomeric Structure ◽  
Chironomus Thummi

Differentiating cells can be characterized by the number and types of proteins they produce (Markert, 1963). In man and other organisms the diversity of hemoglobins has been correlated with ontogenetic changes which reflect the alterations of gene activity (Ingram, 1963). Furthermore, the types of proteins produced are generally specific for the species. The study of insect coelomic proteins has followed closely that of mammalian serum protein analysis; however, profound differences exist between human blood and insect coelomic fluids. For this reason, the term ‘hemolymph’, rather than blood, has been used to designate these fluids. Svedberg & Eriksson-Quensal (1934) first studied the ultracentrifuge properties of Chironomus plumosus hemoglobins and determined them to have a molecular weight of 34000. Braunitzer & Braun (1965) described the multiplicity of hemoglobins in Chironomus thummi and claimed two subunits per molecule. Manwell (1966) suggested the hemoglobins of Chironomus plumosus possessed a monomeric structure.

Routine serum protein analysis by capillary zone electrophoresis: Clinical evaluation

1997 ◽  
Vol 45 (1) ◽  
pp. 390-395 ◽  
Author(s):  
R. Lehmann ◽  
M. Koch ◽  
W. Voelter ◽  
H. U. Häring ◽  
H. M. Liebich
Keyword(s):  
Capillary Zone Electrophoresis ◽  
Serum Protein ◽  
Clinical Evaluation ◽  
Protein Analysis ◽  
Zone Electrophoresis ◽  
Capillary Zone
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