Interaction of Cationic Proteins and Polypeptides with Biocompatible Cationically-Anchored PEG Brushes

2011 ◽  
Vol 44 (20) ◽  
pp. 8161-8168 ◽  
Author(s):  
S. Gon ◽  
B. Fang ◽  
M. M. Santore
Keyword(s):  
Cationic Proteins

scholarly journals POLYMORPHONUCLEAR LEUKOCYTES IN IMMUNOLOGIC REACTIONS

1966 ◽  
Vol 124 (4) ◽  
pp. 733-752 ◽  
Author(s):  
Charles G. Cochrane ◽  
Barbara S. Aikin
Keyword(s):  
Basement Membrane ◽  
Polymorphonuclear Leukocytes ◽  
Electron Microscopic Observation ◽  
Severe Damage ◽  
Electron Microscopic ◽  
Cationic Proteins ◽  
Vascular Basement Membrane ◽  
Arthus Phenomenon ◽  
Immunologic Reactions

Vascular basement membrane was disrupted in the presence of polymorphonuclear leukocytes (PMN's) during two immunologic reactions: The Arthus phenomenon and the reaction to locally injected antibody to vascular basement membrane. This disruption was evidenced by (a) the inability of the basement membrane to retain circulating carbon, by (b) loss of antigenic constituents, and by (c) electron microscopic observation showing actual gaps in the structure of the vascular basement membrane. The factors within PMN's responsible for damage to isolated glomerular basement membrane in vitro were found by isolation procedures to be cathepsins D and E. Cationic proteins of PMN's were separable from the cathepsins. While inducing vascular permeability upon injection, these basic proteins failed to inflict the severe damage to the basement membrane observed in Arthus and antibasement membrane reactions. It is concluded that the full expression of these immunologic lesions requires destruction of the basement membrane possibly brought about by cathepsins D and E. Some of the physicochemical properties of these pathologically active leukocytic factors are given.

Ultrastructural localization of cationic proteins in cytoplasmic granules of chicken and rabbit polymorphonuclear leukocytes

1975 ◽  
Vol 17 (1) ◽  
pp. 79-94
Author(s):  
E.K. Macrae ◽  
J.K. Spitznagel
Keyword(s):  
Polymorphonuclear Leukocytes ◽  
Intracellular Localization ◽  
Ultrastructural Localization ◽  
Cationic Protein ◽  
Cationic Proteins ◽  
Cytoplasmic Granules ◽  
Electron Dense Deposit ◽  
Dense Deposit ◽  
Neutrophilic Polymorphonuclear Leukocytes ◽  
Ammoniacal Silver

Cytoplasmic granules known to contain cationic arginine-rich proteins can be identified by the ammoniacal silver reaction (ASR) which provides a cytochemical marker detectable under the electron microscope. Only the large rod-shaped granules of the chicken polymorphonuclear leukocytes (heterophils) and the large spherical azurophilic granules of the rabbit neutrophilic polymorphonuclear leukocytes show the ASR product as a discrete particulate electron-dense deposit. The other smaller granules are devoid of reaction product, as are membranes and mitochondria. The intracellular localization of the ASR product, as are membranes and mitochondria. The intracellular localization of the ASR product on the large granules coincides with the ASR product localization on the same isolated granule populations, when the ammoniacal silver reaction is applied to these granules after their separation by sucrose-density gradients. The cationic proteins may have intraleukocytic bacteriolytic properties, since ASR product, presumably indicating cationic protein from discharged granules, appears to surround ingested bacteria within cytoplasmic phagosomes.

scholarly journals Comparative study of flocculation and adsorption behaviour of water treatment proteins from Moringa peregrina and Moringa oleifera seeds

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Shirin Nouhi ◽  
Habauka M. Kwaambwa ◽  
Philipp Gutfreund ◽  
Adrian R. Rennie
Keyword(s):  
Amino Acid ◽  
Comparative Study ◽  
Moringa Oleifera ◽  
Seed Proteins ◽  
Adsorption Behaviour ◽  
Separation Processes ◽  
Cationic Proteins ◽  
Considerable Similarity ◽  
Opposite Behavior ◽  
Moringa Peregrina

AbstractTrees of Moringa oleifera are the most widely exploited species of Moringa and proteins extracted from its seeds have been identified as the most efficient natural coagulant for water purification. Largely for climatic reasons, other Moringa species are more accessible in some regions and this paper presents a comparative study of the adsorption to different materials of the proteins extracted from seeds of Moringa peregrina and Moringa oleifera to explore their use as flocculating agents in regions where each is more readily accessible. Results showed that Moringa peregrina seed proteins had higher adsorption to alumina compared to silica, in contrast to opposite behavior for Moringa oleifera. Both species provide cationic proteins that can act as effective coagulants for the various impurities with different surface potential. Despite the considerable similarity of the amino acid composition, the seed proteins have significantly different adsorption and this presents the opportunity to improve processes by choosing the optimal species or combination of species depending on the type of impurity or possible development of separation processes.

scholarly journals Cationic Proteins of Human Granulocytes. II. Separation of the Cationic Proteins of the Granules of Leukemic Myeloid Cells

Blood ◽  
1974 ◽  
Vol 44 (2) ◽  
pp. 235-246 ◽  
Author(s):  
I. Olsson ◽  
P. Venge
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Aminocaproic Acid ◽  
Cationic Protein ◽  
Cationic Proteins ◽  
Molecular Weights ◽  
Electrophoretic Mobilities ◽  
Human Granulocytes ◽  
Protein Components

Abstract The highly cationic proteins of human granulocytes, whose electrophoretic mobilities toward the cathode are faster than that for lysozyme, were isolated from the cytoplasmic granules of leukocytes, obtained from patients with chronic myeloid leukemia. The granule extract was subjected to chromatography on Sephadex G-75 and E-aminocaproic acid-Sepharose ion adsorbant followed by preparative electrophoresis on agarose. Seven cationic protein components were identified, and five of these were obtained in a pure form. One group of cationic proteins, including components 1-4, exhibited molecular weights in the range 25,500-28,500, almost identical amino acid composition, and complete immunologic identity. Another group of proteins, including components 5-7, exhibited molecular weights in the range 21,000-29,000 and also showed complete immunologic identity; amino acid analysis performed on component 5 indicated a different amino acid composition from that of components 1-4. Cationic proteins with similar electrophoretic mobilities and immunochemical identities were also detected in granule extracts of granulocytes from healthy individuals. The proteins isolated from human granulocytes have a higher molecular weight and a lower content of basic amino acids than the cationic proteins with antibacterial and permeability-increasing properties previously demonstrated in rabbit polymorphonuclear granulocytes.

Cationic detergent in agarose for improved electrophoresis of cationic proteins

1991 ◽  
Vol 12 (1) ◽  
pp. 96-99 ◽  
Author(s):  
Claus M. Reimert ◽  
Thorkild C. Bøg-Hansen
Keyword(s):  
Cationic Proteins ◽  
Cationic Detergent

Binding Sites for Cationic Proteins on Staphylococci

1972 ◽  
Vol 13 (5) ◽  
pp. 501-502 ◽  
Author(s):  
W.G. MacMillan ◽  
K.G. Hibbitit
Keyword(s):  
Binding Sites ◽  
Cationic Proteins
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