Further Characterization of Surface Membrane Structures Expressed on Human Basophils and Mast Cells

1990 ◽  
Vol 91 (2) ◽  
pp. 198-203 ◽  
Author(s):  
Peter Valent ◽  
Otto Majdic ◽  
Dieter Maurer ◽  
Michael Bodger ◽  
Manfred Muhm ◽  
...  
Keyword(s):  
Mast Cells ◽  
Surface Membrane ◽  
Membrane Structures ◽  
Human Basophils

scholarly journals Characterization of LDL and VLDL Binding Sites on Human Basophils and Mast Cells

1995 ◽  
Vol 15 (1) ◽  
pp. 17-26 ◽  
Author(s):  
Irene Virgolini ◽  
Shu-Ren Li ◽  
Qiong Yang ◽  
Elisabeth Koller ◽  
Wolfgang R. Sperr ◽  
...  
Keyword(s):  
Mast Cells ◽  
Binding Sites ◽  
Human Basophils

Characterization of Citrullination Sites in Neutrophils and Mast Cells Activated by Ionomycin via Integration of Mass Spectrometry and Machine Learning

2021 ◽  
Author(s):  
Raghothama Chaerkady ◽  
Yebin Zhou ◽  
Jared A. Delmar ◽  
Shao Huan Samuel Weng ◽  
Junmin Wang ◽  
...  
Keyword(s):  
Machine Learning ◽  
Mass Spectrometry ◽  
Mast Cells

scholarly journals Ultrastructural Studies of Human Basophils and Mast Cells

2005 ◽  
Vol 53 (9) ◽  
pp. 1043-1070 ◽  
Author(s):  
Ann M. Dvorak
Keyword(s):  
Growth Factor ◽  
Mast Cells ◽  
Cord Blood ◽  
Blood Cells ◽  
De Novo ◽  
Ultrastructural Studies ◽  
Specific Growth Factor ◽  
Cord Blood Cells ◽  
Human Basophils

Ultrastructural studies of human mast cells (HMCs) and basophils (HBs) are reviewed. Sources of HMCs include biopsies of tissue sites and in situ study of excised diseased organs; isolated, partially purified samples from excised organs; and growth-factor-stimulated mast cells that develop de novo in cultures of cord blood cells. Sources of HBs for study include partially purified peripheral blood basophils, basophils in tissue biopsies, and specific growth factor-stimulated basophils arising de novo from cord blood cells. The ultrastructural studies reviewed deal with identity, secretion, vesicles, recovery, and synthesis issues related to the biology of these similar cells.

scholarly journals Cytochemical localization of a "basic" ATPase to canine myocardial surface membrane.

1980 ◽  
Vol 28 (12) ◽  
pp. 1286-1294 ◽  
Author(s):  
N N Malouf ◽  
G Meissner
Keyword(s):  
Cardiac Muscle ◽  
Microsomal Fraction ◽  
Surface Membrane ◽  
Buoyant Density ◽  
Membrane Structures ◽  
Intercalated Disc ◽  
Cytochemical Localization ◽  
Fixed Tissue ◽  
T System

Enzymatic properties of a canine cardiac muscle microsomal fraction were determined to localize in situ a "basic," divalent cation dependent adenosine triphosphatase (ATPase) by ultrastructural cytochemistry. The microsomal fraction had a buoyant density of 1.08--1.13 (20--30% [w/w] sucrose) and hydrolyzed adenosine triphosphate in the presence of Mg2+, Ca2+, Mn2+, or Co2+, but not in that of Sr2+ or Ni2+, under conditions that inhibited interfering (Na+ + K+)-ATPase and sarcoplasmic reticulum Ca2+-ATPase activities. "Basic" ATPase was localized in paraformaldehyde-fixed tissue in a medium containing Mg2+ or a high Ca2+ concentration (4 mM). A free Pb2+ concentration of less than 1 microM was used to capture enzymatically released phosphate anions. Electron-dense lead precipitates were present at the plasmalemma, T-system, and intercalated disc membranes with the exception of the nexus. These studies suggest that "basic" ATPase activity is associated with surface membrane structures of canine cardiac muscle.

Physicochemical Characterization of Transport in Nanosized Membrane Structures

ChemPhysChem ◽  
2010 ◽  
Vol 11 (2) ◽  
pp. 404-411 ◽  
Author(s):  
Siavash Darvishmanesh ◽  
Jan Degrève ◽  
Bart Van der Bruggen
Keyword(s):  
Physicochemical Characterization ◽  
Membrane Structures
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