I= PRIMARY STRUCTURE OF HEMOGLOBIN'S (A) ABNORMAL HUMAN MEMOGLOBINS (B) HEMOGLOBINS FROM JAGAR (PANTHERA ONCO) & LEOPARD (PANTHERA PARDUS)
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Title of Thesis
PRIMARY STRUCTURE OF HEMOGLOBIN'S (A) ABNORMAL HUMAN MEMOGLOBINS (B) HEMOGLOBINS FROM JAGAR (PANTHERA ONCO) & LEOPARD (PANTHERA PARDUS)

Author(s)
Aftab Ahmed
Institute/University/Department Details
University of Karachi/ H.E.J. Research Institute of Chemistry
Session
1988
Subject
Chemistry
Number of Pages
110
Keywords (Extracted from title, table of contents and abstract of thesis)
hemoglobin, memoglobins, jagar (panthera onco), leopard (panthera pardus), globin chains, hemoglobin structure, mammalian hemoglobins, thalassemia

Abstract
The present study on abnormal hemoglobin's, jaguar (panthera onco) and North Persian leopard (panthera pardus) hemoglobins were undertaken to characterize the abnormality in the hemoglobin variants and the primary structure of globin chains respectively.

Different electrophoretic methods i.e. cellulose acetate membrance Polyacrylamide gel disc, isoelectric focusing in thin layer IEE gel and Trition-PAG were used to identify the hemoglobin components and the globin chains.

Hemoglobin components and globin chains were isolated on DEAE-Sephacel and CM-Cellulose in the presence of dissociating agent 8M urea respectively.

Reversed phase HPLC was employed successfully for the isolation of the globin chains and the fingerprinting of tryptic peptides.

The complete primary structures of abnormal peptides and of the globin chains were established by using the liquid and gas-phase sequencer.

Sequence study on abnormal hemoglobins results in the characterization of three variants. 1).Hb-Ea2b226Glu-Lys inassocation with B-thalassemia disorder. 2).A new hemoglobin vartiant Hb-karachi a2B2. 3).Hb-Andrew-Minneapolis a2B2 144Lys-Asn in a German family (Father and his son) from berlin.

The study on animal hemoglobin results in the characterization of 6 globin chains i.e. one alpha, and two B-chains in each animal. The sequence alignment with the members of the family felidae reveals high degree of homology both in the and chains.

Download Full Thesis
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S. No. Chapter Title of the Chapters Page Size (KB)
1 0 Contents
83.95 KB
2 1 Introduction 1
148.61 KB
  1.1 General Introduction 1
  1.2 Respiratory Function of Hemoglobin 2
  1.3 Hemoglobin structure 3
  1.4 Synthesis of hemoglobin 4
  1.5 Hemoglobinopathies 5
  1.6 Genetic aspect of bnornal hemoglobins 7
  1.7 Mammalian hemoglobins 9
  1.8 Evolution and phylogeny 11
  1.9 Objective of present studies 14
3 2 Experimental 14
127.24 KB
  2.1 Collection of blood samples 15
  2.2 Isolation of hemoglobin 15
  2.3 Preparation of globin 16
  2.4 Electrophoresis 16
  2.5 Separation of hemoglobin components 19
  2.6 Separation of globin chains 20
  2.7 Ion-exchange chromatography 20
  2.8 Enzymatic digestion 22
  2.9 Separation of tryptic peptides 22
  2.10 Thin layer electrophoresis 23
  2.11 Automatic amino acid analysis 24
  2.12 FAB-mass spectroscopy 24
  2.13 Amino acid sequencing 25
4 3 Results 29
342.26 KB
  3.1 hemoglobin E B-Thalassemia 29
  3.2 Hemoglobin Karachi 38
  3.3 Hemoglobin AndrewMinnwapolis 44
  3.4 Jaguar hemoglobins 53
  3.5 North Persian leopard hemoglobins 66
5 4 Discussion 78
143.92 KB
  4.1 hemoglobin E B-Thalassemia 78
  4.2 Hemoglobin Karachi 79
  4.3 Hemoglobin Andrew-Minneapolis 81
  4.4 Carnivora hemoglobin’s 83
6 5 References 97
112.71 KB