Influence of Phytate Removal and Structural Modification on the Calcium-binding Properties of Soybean Globulins

1998 ◽  
Vol 62 (2) ◽  
pp. 341-346 ◽  
Author(s):  
Hitomi KUMAGAI ◽  
Yoshiharu SHIZAWA ◽  
Hidetoshi SAKURAI ◽  
Hitoshi KUMAGAI
Keyword(s):  
Calcium Binding ◽  
Structural Modification ◽  
Binding Properties ◽  
Soybean Globulins

scholarly journals The calcium-binding properties of bovine factor V.

1980 ◽  
Vol 255 (2) ◽  
pp. 638-645 ◽  
Author(s):  
L.S. Hibbard ◽  
K.G. Mann
Keyword(s):  
Calcium Binding ◽  
Factor V ◽  
Binding Properties ◽  
Bovine Factor

scholarly journals Tuning Anion-Binding Properties of 22-Membered Unclosed Cryptands by Structural Modification of the Lariat Arm

ACS Omega ◽  
2020 ◽  
Vol 5 (45) ◽  
pp. 29601-29608
Author(s):  
Kajetan Dąbrowa ◽  
Patryk Niedbała ◽  
Marcin Pawlak ◽  
Marcin Lindner ◽  
Wiktor Ignacak ◽  
...  
Keyword(s):  
Structural Modification ◽  
Anion Binding ◽  
Binding Properties

Calcium Binding Properties of an Epidermal Growth Factor-like Domain Pair from Human Fibrillin-1

1996 ◽  
Vol 255 (1) ◽  
pp. 22-27 ◽  
Author(s):  
Vroni Knott ◽  
Kristina A. Downing ◽  
Caroline M. Cardy ◽  
Penny Handford
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Calcium Binding ◽  
Domain Pair ◽  
Binding Properties ◽  
Fibrillin 1 ◽  
Epidermal Growth

scholarly journals Calcium-binding properties of SSP-5, the Streptococcus gordonii M5 receptor for salivary agglutinin.

1994 ◽  
Vol 62 (12) ◽  
pp. 5220-5226 ◽  
Author(s):  
Y Duan ◽  
E Fisher ◽  
D Malamud ◽  
E Golub ◽  
D R Demuth
Keyword(s):  
Calcium Binding ◽  
Streptococcus Gordonii ◽  
Binding Properties

HALOTHANE AND ISOFLURANE ALTER THE CALCIUM BINDING PROPERTIES OF CALMODULIN

1994 ◽  
Vol 81 (SUPPLEMENT) ◽  
pp. A886
Author(s):  
T. J. J. Blanck ◽  
A. Levin
Keyword(s):  
Calcium Binding ◽  
Binding Properties

Calcium Binding Properties of Vitamin K-Dependent Clotting Factors

1993 ◽  
pp. 3-13 ◽  
Author(s):  
J. Stenflo ◽  
M. Selander ◽  
E. Persson ◽  
J. Astermark ◽  
C. Valcarce ◽  
...  
Keyword(s):  
Vitamin K ◽  
Calcium Binding ◽  
Clotting Factors ◽  
Binding Properties

Recalculation of calcium-binding properties of human and rat fibrin(ogen) and their degradation products

1981 ◽  
Vol 22 (5-6) ◽  
pp. 653-657 ◽  
Author(s):  
Willem Nieuwenhuizen ◽  
Irina A.M. van Ruijven-Vermeer ◽  
Willem J. Nooijen ◽  
Anton Vermond ◽  
Frits Haverkate ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Degradation Products ◽  
Binding Properties

scholarly journals Toxoplasma modifies macrophage phagosomes by secretion of a vesicular network rich in surface proteins.

1986 ◽  
Vol 103 (3) ◽  
pp. 867-874 ◽  
Author(s):  
L D Sibley ◽  
J L Krahenbuhl ◽  
G M Adams ◽  
E Weidner
Keyword(s):  
Electron Microscopy ◽  
Cell Surface ◽  
Polyclonal Antibody ◽  
Calcium Binding ◽  
Structural Modification ◽  
Surface Proteins ◽  
Structural Proteins ◽  
Toxoplasma Infection ◽  
Sds Page ◽  
Structural Matrix

Modification of macrophage phagosomes begins shortly after formation as Toxoplasma cells secrete membranous vesicles that form a reticulate network within the vacuole. The Toxoplasma-modified compartments then resist normal endocytic processing and digestion. We have used the pronounced Ca++-dependent stability of the intraphagosomal membrane (IPM) network to purify and characterize the structural proteins of this assembly. In addition to the structural matrix, Toxoplasma secretes a discrete set of soluble proteins, including a newly described 22-kD calcium-binding protein. The IPM network adheres to intact Toxoplasma cells after host cell lysis in the presence of 1 mM Ca++; however, the network readily disperses in calcium-free buffer and was purified as vesicles that sedimented at 100,000 g. Purified IPM vesicles were specifically recognized by immune sera from mice with chronic Toxoplasma infection and consisted primarily of a 30-kD protein when analyzed by SDS PAGE. IPM network proteins share a major antigenic component located on the surface of extracellular Toxoplasma cells as shown by immunoperoxidase electron microscopy using a polyclonal antibody prepared against the IPM vesicles. Moreover, in Toxoplasma-infected macrophages, anti-IMP antibody confirmed that the extensive IPM array contains proteins also found on the Toxoplasma cell surface. Our results indicate the IMP network represents a unique structural modification of the phagosome comprised in part of Toxoplasma surface proteins.

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