scholarly journals An Alternative to the Human Hemoglobin Test in the Investigation of Bloodstains Treated with Active Oxygen: The Human Glycophorin A Test

2011 ◽  
Vol 11 ◽  
pp. 907-916 ◽  
Author(s):  
Ana Castelló ◽  
Francesc Francés ◽  
Fernando Verdú
Keyword(s):  
Human Blood ◽  
Biological Fluid ◽  
Active Oxygen ◽  
Glycophorin A ◽  
Human Hemoglobin ◽  
False Negatives ◽  
Destructive Effect ◽  
Confirmatory Tests ◽  
Three Stages ◽  
Human Glycophorin

In criminal investigations, there are three stages involved when studying bloodstains: search and orientation, confirmation, and individualization. Confirmatory tests have two aims: to show that the stain contains a human biological fluid and to confirm the type of biological fluid. The need to determine the nature of the evidence is reflected in the latest bibliography, where the possibility of employing mRNA and miRNA markers for this purpose is proposed. While these new proposals are being investigated, the kits for determining human hemoglobin currently provide a simple solution for resolving this issue. With these kits, the possibility of obtaining false positives and false negatives is well known. However, recently, a new problem has been detected. This involves the interference caused by new cleaning products that contain sodium percarbonate (or active oxygen) when determining human hemoglobin. With the aim to resolve this problem, this work studied the ability of the human glycophorin A test to determine human blood in samples that have been treated with active oxygen. Our results show that the human glycophorin A test has a greater resistance to the destructive effect of the new detergents containing active oxygen; consequently, it provides an alternative to be taken into consideration in the confirmatory diagnoses of bloodstains.

scholarly journals Structural variation of the malaria-associated human glycophorin A-B-E region

BMC Genomics ◽  
2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Sandra Louzada ◽  
Walid Algady ◽  
Eleanor Weyell ◽  
Luciana W. Zuccherato ◽  
Paulina Brajer ◽  
...  
Keyword(s):  
Structural Variation ◽  
Glycophorin A ◽  
E Region ◽  
Human Glycophorin

scholarly journals The mechanism of production of multiple mRNAs for human glycophorin A

1990 ◽  
Vol 18 (19) ◽  
pp. 5829-5836 ◽  
Author(s):  
Jawed Hamid ◽  
Alfred T.H. Burness
Keyword(s):  
Glycophorin A ◽  
Human Glycophorin

scholarly journals Hemolymph of molluscan origin: from biochemistry to modern biomaterials science

2020 ◽  
Vol 127 (1) ◽  
Author(s):  
Tomasz Machałowski ◽  
Teofil Jesionowski
Keyword(s):  
Immune Response ◽  
Human Blood ◽  
Body Fluid ◽  
Biological Fluid ◽  
Shell Formation ◽  
Future Directions ◽  
Material Chemistry ◽  
Biomineralization Process ◽  
Points Of View ◽  
First Time

AbstractMolluscan hemolymph is a unique kind of body fluid, which in many respects is analogous to human blood, although there are several crucial differences. Here, for the first time, we critically analyze the prospects for applications of this fluid in modern biomaterials science. Particular attention is paid to the biochemistry and chemistry of molluscan hemolymph, as well as to hemocytes and hemocyanins as key functional players within this unique biological fluid. We focus on hemocytes as multifunctional hemolytic cells involved in immune response, and especially in the biomineralization process. The next part of the review contains a discussion of molluscan shell formation and regeneration from different points of view. Finally, we consider the challenges, solutions, and future directions in the application of molluscan hemolymph for bioinspired material chemistry and biomedicine.

Determination of single monosugars bound to a peptide.

1997 ◽  
Vol 44 (2) ◽  
pp. 285-291
Author(s):  
H Krotkiewski ◽  
B Krotkiewska
Keyword(s):  
Degradation Products ◽  
Internal Standard ◽  
Gas Liquid Chromatography ◽  
Glycophorin A ◽  
Weakly Alkaline ◽  
Alkaline Conditions ◽  
Beta Elimination ◽  
Ovine Submaxillary Mucin ◽  
Human Glycophorin

A method is described which allows detection and quantitative determination of single monosugar units bound O-glycosidically to a peptide. A glycoprotein or a glycopeptide is chemically degraded under the modified conditions of Carlson degradation (beta-elimination performed in weakly alkaline conditions in the presence of sodium borohydride). An aliquot of the neutralized reaction mixture, supplemented with an internal standard, is peracetylated, extracted and directly analyzed by g.l.c.-m.s. All the O-linked oligosaccharides split off from the peptide are derivatized, but under gas-liquid chromatography at 150-230 degrees C only monosugar peracetylated alditols reach the detector. By comparing the retention times of appropriate peaks with standards and by checking their mass spectra the monosugar alditols are unequivocally identified. The detectable amount of a reduced monosugar in the analyzed sample is about 0.3 microgram. Several glycoproteins were analyzed using this method. Free N-acetylgalactosaminitol was detected in the degradation products of human glycophorin A and ovine submaxillary mucin, additionally free galactitol was detected in the degradation products of glycophorin. This result suggests that some single galactose units, O-glycosidically linked to the peptide are present in human glycophorin A.

Mouse models of IgG- and IgM-mediated hemolysis

Blood ◽  
2006 ◽  
Vol 109 (7) ◽  
pp. 3099-3107 ◽  
Author(s):  
David A. Schirmer ◽  
Shuh-Chyung Song ◽  
Jeffrey P. Baliff ◽  
Stephanie O. Harbers ◽  
Raphael A. Clynes ◽  
...  
Keyword(s):  
Mouse Models ◽  
Passive Immunization ◽  
Glycophorin A ◽  
Blood Group System ◽  
Intravascular Hemolysis ◽  
Fcγ Receptors ◽  
Rapid Clearance ◽  
The Complement System ◽  
Insight Into ◽  
Human Glycophorin

Abstract Well-characterized mouse models of alloimmune antibody-mediated hemolysis would provide a valuable approach for gaining greater insight into the pathophysiology of hemolytic transfusion reactions. To this end, mouse red blood cells (mRBCs) from human glycophorin A transgenic (hGPA-Tg) donor mice were transfused into non-Tg recipients that had been passively immunized with IgG or IgM hGPA-specific monoclonal antibodies (mAbs). In this novel murine “blood group system,” mRBCs from hGPA-Tg mice are “antigen positive” and mRBCs from non-Tg mice are “antigen negative.” Passive immunization of non-Tg mice with the IgG1 10F7 and IgG3 NaM10-2H12 anti-hGPA mAbs each induced rapid clearance of incompatible transfused hGPA-Tg-mRBCs in a dose-response manner. Using various knockout mice as transfusion recipients, both the complement system and activating Fcγ receptors were found to be important in the clearance of incompatible mRBCs by each of these IgG mAbs. In addition, the IgM E4 anti-hGPA mAb induced complement-dependent intravascular hemolysis of transfused incompatible hGPA-Tg-mRBCs accompanied by gross hemoglobinuria. These initial studies validate the relevance of these new mouse models for addressing important questions in the field of transfusion medicine.

Sign in / Sign up

Export Citation Format

Share Document