http://habibiaislamicus.com/index.php/hirj/article/view/22900

2021 ◽  
Vol 5 (2) ◽  
pp. 15-20
Keyword(s):  
Amino Acid ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Building Block ◽  
Red Meat ◽  
Body Building ◽  
Biological Importance ◽  
Special Children ◽  
The Way

Red meat is considered to be important part of our diet, as it helps in making of blood specially red blood cell which circulates oxygen in our body and it also important part of our body building block as amino acid is use for making of DNA. The objective of this research is not to discuss its biological importance but to clear the objection of other religion towards the way of slaughtering in Islam. And also clear the awareness of slaughtering between each individual Muslim, Non-Muslim and special children

scholarly journals http://jibas.org/index.php/jibas/article/view/4

JIBAS ◽  
2021 ◽  
Vol 1 (1) ◽  
pp. 15-20
Author(s):  
Maham Ghauri ◽  
Keyword(s):  
Amino Acid ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Building Block ◽  
Red Meat ◽  
Body Building ◽  
Biological Importance ◽  
Special Children ◽  
The Way

Red meat is considered to be important part of our diet, as it helps in making of blood specially red blood cell which circulates oxygen in our body and it also important part of our body building block as amino acid is use for making of DNA. The objective of this research is not to discuss its biological importance but to clear the objection of other religion towards the way of slaughtering in Islam. And also clear the awareness of slaughtering between each individual Muslim, Non-Muslim and special children.

In vitro effects of temperature on red blood cell deformability and membrane stability in human and various vertebrate species

2021 ◽  
pp. 1-10
Author(s):  
Adam Attila Matrai ◽  
Gabor Varga ◽  
Bence Tanczos ◽  
Barbara Barath ◽  
Adam Varga ◽  
...  
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Whole Blood ◽  
Mechanical Stability ◽  
Cell Deformability ◽  
Blood Samples ◽  
Effects Of Temperature ◽  
The Way ◽  
Rbc Deformability

BACKGROUND: The effects of temperature on micro-rheological variables have not been completely revealed yet. OBJECTIVE: To investigate micro-rheological effects of heat treatment in human, rat, dog, and porcine blood samples. METHODS: Red blood cell (RBC) - buffer suspensions were prepared and immersed in a 37, 40, and 43°C heat-controlled water bath for 10 minutes. Deformability, as well as mechanical stability of RBCs were measured in ektacytometer. These tests were also examined in whole blood samples at various temperatures, gradually between 37 and 45°C in the ektacytometer. RESULTS: RBC deformability significantly worsened in the samples treated at 40 and 43°C degrees, more expressed in human, porcine, rat, and in smaller degree in canine samples. The way of heating (incubation vs. ektacytometer temperation) and the composition of the sample (RBC-PBS suspension or whole blood) resulted in the different magnitude of RBC deformability deterioration. Heating affected RBC membrane (mechanical) stability, showing controversial alterations. CONCLUSION: Significant changes occur in RBC deformability by increasing temperature, showing inter-species differences. The magnitude of alterations is depending on the way of heating and the composition of the sample. The results may contribute to better understanding the micro-rheological deterioration in hyperthermia or fever.

The Design and Preparation of a Model Spectrin Protein: βII-Spectrin L2079P

2010 ◽  
Vol 4 (1) ◽  
Author(s):  
N. Palmer ◽  
A. Antoniou ◽  
L.W.M. Fung
Keyword(s):  
Amino Acid ◽  
Recombinant Protein ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Structural Difference ◽  
Cytoskeletal Proteins ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Specific Proteins ◽  
Brain Spectrin

Spectrin isoforms are cytoskeletal proteins that give stability to cells. Site directed mutagenesis was used to replace residue 2079 in brain spectrin βII from leucine to proline, the corresponding amino acid in red blood cell spectrin βI. We have shown previously that, in spectrin βI, the region downstream of the proline residue is unstructured, whereas the corresponding region in spectrin βII (downstream of a leucine residue) appears to be helical. This structural difference has been suggested to be responsible for binding specific proteins to each β-spectrin isoform, with G5 only to βI-spectrin and F11 only to βII-spectrin. Thus, it is possible that the mutation from leucine to proline in βII-spectrin may lead to a conformational change in βII, from helical to unstructured. In this study, a recombinant protein consisting of a fragment of II-spectrin, with L2079P mutation, has been designed and prepared.

The importance of a single amino acid substitution in reduced red blood cell carbonic anhydrase function of early-diverging fish

2020 ◽  
Vol 190 (3) ◽  
pp. 287-296
Author(s):  
Angelina M. Dichiera ◽  
Olivia J. L. McMillan ◽  
Alexander M. Clifford ◽  
Greg G. Goss ◽  
Colin J. Brauner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Blood Cell ◽  
Amino Acid Substitution ◽  
Red Blood Cell ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid

scholarly journals Primary structure of murine red blood cell-type pyruvate kinase (PK) and molecular characterization of PK deficiency identified in the CBA strain

Blood ◽  
1995 ◽  
Vol 86 (8) ◽  
pp. 3205-3210 ◽  
Author(s):  
H Kanno ◽  
M Morimoto ◽  
H Fujii ◽  
T Tsujimura ◽  
H Asai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Blood Cell ◽  
Missense Mutation ◽  
Pyruvate Kinase ◽  
Red Blood Cell ◽  
Cdna Sequence ◽  
Amino Acid Change ◽  
Mutant Mice ◽  
Cell Type ◽  
Blood Cell Type

Abstract To clarify the molecular abnormality of pyruvate kinase (PK) deficiency identified in the mutant mice of CBA-Pk-1slc/Pk-1slc, we cloned murine red blood cell-type PK (R-PK) cDNA of those animals. The cDNA sequence spans 1827 bp, including an open reading frame that can encode 574 amino acids. Homology in the coding sequences between murine and human R-PK was 86.1% at nucleotide and 91.5% at amino acid levels. A homozygous missense mutation at nucleotide 1013 GGT-->GAT was identified in the cDNA sequence of the mutant, causing a single amino acid substitution at no. 338Gly-->Asp of the murine R-PK. Six amino acid residues, 335Val-336Ala-337Arg-338Gly-339Asp-340L eu, were encoded in exon 8 of both human and rat L (liver-type)/R-PK genes and were evolutionarily conserved in PK from bacteria through humans. 337Arg was reported to be important for substrate binding, suggesting that the amino acid change would impair substrate affinity of the PK subunit. A homozygous missense mutation at the catalytic domain has been identified in a human PK variant, PK Hong Kong (941ATT-->ACT, 314 Ile-- >Thr). Although both 1013A and 941C gave rise to an amino acid change adjacent to the active site and may interfere with substrate binding to the subunit, the degree of anemia was much more severe in the human case. The erythroid-progenitor cell number increased in the spleen of Pk-1slc/Pk-1slc mice to a level approximately 66 times higher than that in normal CBA mice, suggesting that compensatory extramedullary erythropoiesis in the spleen of the mutant mice, but not in the human variant, might account for the observed difference in the phenotype.

Alterations in red blood cell parameters, plasma amino acids, total cholesterol and fatty acids in Standardbred horses undergoing fitness training

2019 ◽  
Vol 15 (1) ◽  
pp. 13-23 ◽  
Author(s):  
R.H. Dunstan ◽  
M.M. Macdonald ◽  
A. Marks ◽  
D.L. Sparkes ◽  
T.K. Roberts
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Exercise Training ◽  
Blood Cell ◽  
Stearic Acid ◽  
Palmitic Acid ◽  
Red Blood Cell ◽  
Training Period ◽  
Weekly Basis ◽  
Cell Counts

Maintenance of metabolic homeostasis is vital to optimise the supply of nutrients to support exercise and facilitate recovery and repair processes in horses. This study assessed the effects of exercise on resting plasma homeostasis in horses upon initiation of a training program to attain fitness in preparation for competitive harness racing. Four Standardbred horses (three males and one female) that had not been in work for at least 6 months were assessed prior to the commencement of the training program and then progressively on a weekly basis for 8 weeks. Resting plasma samples were collected in the early morning prior to exercise training and feeding. Samples were analysed for amino acid composition, cholesterol, palmitic acid and stearic acid on a weekly basis, and red blood cell counts and haemoglobin were analysed at weeks 0, 4 and 8. The red cell counts and levels of haemoglobin increased progressively over the training period (P<0.05). Specific amino acids in the plasma displayed temporal variations during the training period. Glycine was the most abundant amino acid in resting horse plasma and together with serine was reduced throughout the first half of the training period, eventually returning to initial levels at weeks 7 and 8 (P<0.05). A number of amino acids were noted to increase in concentration throughout the 8 week training period including ornithine, histidine and hydroxyproline (P<0.05). Cholesterol fell to substantially lower levels after 8 weeks of exercise (P<0.05). Palmitic acid showed three ‘peaks’ of elevated concentrations in plasma (P<0.05) following the initiation of exercise and then again at the transitions into harder fast work sessions. Stearic acid was relatively constant throughout the exercise period. Adjustments in the plasma composition of these key metabolites were consistent with supporting the increased metabolic demands associated with the higher levels of exercise training.

scholarly journals Primary structure of murine red blood cell-type pyruvate kinase (PK) and molecular characterization of PK deficiency identified in the CBA strain

Blood ◽  
1995 ◽  
Vol 86 (8) ◽  
pp. 3205-3210 ◽  
Author(s):  
H Kanno ◽  
M Morimoto ◽  
H Fujii ◽  
T Tsujimura ◽  
H Asai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Blood Cell ◽  
Missense Mutation ◽  
Pyruvate Kinase ◽  
Red Blood Cell ◽  
Cdna Sequence ◽  
Amino Acid Change ◽  
Mutant Mice ◽  
Cell Type ◽  
Blood Cell Type

To clarify the molecular abnormality of pyruvate kinase (PK) deficiency identified in the mutant mice of CBA-Pk-1slc/Pk-1slc, we cloned murine red blood cell-type PK (R-PK) cDNA of those animals. The cDNA sequence spans 1827 bp, including an open reading frame that can encode 574 amino acids. Homology in the coding sequences between murine and human R-PK was 86.1% at nucleotide and 91.5% at amino acid levels. A homozygous missense mutation at nucleotide 1013 GGT-->GAT was identified in the cDNA sequence of the mutant, causing a single amino acid substitution at no. 338Gly-->Asp of the murine R-PK. Six amino acid residues, 335Val-336Ala-337Arg-338Gly-339Asp-340L eu, were encoded in exon 8 of both human and rat L (liver-type)/R-PK genes and were evolutionarily conserved in PK from bacteria through humans. 337Arg was reported to be important for substrate binding, suggesting that the amino acid change would impair substrate affinity of the PK subunit. A homozygous missense mutation at the catalytic domain has been identified in a human PK variant, PK Hong Kong (941ATT-->ACT, 314 Ile-- >Thr). Although both 1013A and 941C gave rise to an amino acid change adjacent to the active site and may interfere with substrate binding to the subunit, the degree of anemia was much more severe in the human case. The erythroid-progenitor cell number increased in the spleen of Pk-1slc/Pk-1slc mice to a level approximately 66 times higher than that in normal CBA mice, suggesting that compensatory extramedullary erythropoiesis in the spleen of the mutant mice, but not in the human variant, might account for the observed difference in the phenotype.

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