Δ-Aminolevulinic Acid Synthetase Activity in Normal Human Bone Marrow and in Patients with Idiopathic Sideroblastic Anemia

Enzyme ◽  
1973 ◽  
Vol 16 (1-6) ◽  
pp. 138-145 ◽  
Author(s):  
S.S. Bottomley ◽  
M. Tanaka ◽  
J. Self
Keyword(s):  
Bone Marrow ◽  
Aminolevulinic Acid ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Synthetase Activity ◽  
Sideroblastic Anemia ◽  
Normal Human ◽  
Normal Human Bone Marrow

scholarly journals Characterization and Measurement of Heme Synthetase in Normal Human Bone Marrow

Blood ◽  
1968 ◽  
Vol 31 (3) ◽  
pp. 314-322 ◽  
Author(s):  
SYLVIA S. BOTTOMLEY
Keyword(s):  
Bone Marrow ◽  
Enzymatic Reaction ◽  
Enzyme Concentration ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Synthetase Activity ◽  
Ph Optimum ◽  
Normal Human ◽  
Negative Feedback Control ◽  
Normal Human Bone Marrow

Abstract The heme synthetase step in human bone marrow has been characterized in a crude lysate as an enzymatic reaction in that it has a pH optimum of 7.4, is heat labile, and at optimum substrate concentrations is linear with time and enzyme concentration over the first 30 minutes. The Km of iron was found to be 1.7 x 10-5M and for protoporphyrin 1.8 x 10-6M. High iron concentrations do not affect the enzyme but ascorbic acid and glutathione were found to augment the activity of the enzyme. Pyridoxine and high protoporphyrin concentrations inhibit heme synthetase activity. A negative feedback control of heme synthetase by heme is present in human red cell precursors.

FRACTIONATION OF NORMAL HUMAN BONE MARROW ON ALBUMIN GRADIENTS

1974 ◽  
Vol 52 (5) ◽  
pp. 767-778 ◽  
Author(s):  
KA Rickard ◽  
L Dunleavy ◽  
R Brown ◽  
H Kronenberg
Keyword(s):  
Bone Marrow ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Normal Human ◽  
Normal Human Bone Marrow

Activators and inhibitors of fibrinolysis in normal human bone marrow

1995 ◽  
Vol 6 (2) ◽  
pp. 167
Author(s):  
Nicola A. McWilliam ◽  
Nuala A. Booth ◽  
Linda A. Robbie ◽  
Bruce Bennett
Keyword(s):  
Bone Marrow ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Normal Human ◽  
Normal Human Bone Marrow

scholarly journals Fractionation of subsets of BFU-E from normal human bone marrow: responsiveness to erythropoietin, human placental-conditioned medium, or granulocyte-macrophage colony-stimulating factor

Blood ◽  
1988 ◽  
Vol 71 (3) ◽  
pp. 758-765 ◽  
Author(s):  
G Kannourakis ◽  
GR Johnson
Keyword(s):  
Bone Marrow ◽  
Conditioned Medium ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Colony Stimulating Factor ◽  
Normal Human ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor ◽  
Normal Human Bone Marrow

Abstract Normal human bone marrow mononuclear cells were fractionated by differential adherence, immunomagnetic separation, and fluorescence- activated cell sorting (FACS). The resultant fractionated cells were cultured in semisolid medium to monitor the presence of BFU-E, Mix-CFC, and nonerythroid CFC. Two populations of cells were recovered on the basis of binding by the monoclonal antibody (MoAb) RFB-1. One of these populations contained BFU-E that were stimulated only by erythropoietin (Epo), whereas the second population contained BFU-E responsive to Epo, Epo and recombinant human granulocyte-macrophage colony-stimulating factor (rHGM-CSF), or Epo and human placental-conditioned medium (HPCM). Prior enrichment of clonogenic cells by removal of adherent and Leu-M3+ve, Leu-4+ve, Leu-7+ve, B1+ve, WEMG1+ve, and Glycophorin A+ve cells, followed by FACS fractionation on the basis of RFB-1 binding, consistently resulted in recoveries of BFU-E, Mix-CFC, and nonerythroid CFC of greater than 100% (up to 800%). These procedures also resulted in enrichment of up to 200-fold and frequencies of 1:6 for BFU-E, 1:5 for CFC, and 1:130 for Mix-CFC.

scholarly journals Cytochemical Localization of an Adenosine Triphosphate Dephosphorylating Enzyme in the Granules of Human Eosinophils

Blood ◽  
1962 ◽  
Vol 19 (5) ◽  
pp. 612-614 ◽  
Author(s):  
DAVID WEINSTEIN ◽  
J. R. SOMMER ◽  
J. W. BEARD
Keyword(s):  
Bone Marrow ◽  
Adenosine Triphosphate ◽  
Myeloid Cells ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Cytochemical Localization ◽  
Normal Human ◽  
Normal Human Bone Marrow

Abstract The granules of the eosinophilic myeloid cells of normal human bone marrow exerted a pronounced activity to dephosphorylate adenosine triphosphate. This behavior was not shown by the granules of other myeloid cells.

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