scholarly journals Membrane isolation on polylysine-coated beads. Plasma membrane from HeLa cells.

1977 ◽  
Vol 75 (1) ◽  
pp. 119-134 ◽  
Author(s):  
C M Cohen ◽  
D I Kalish ◽  
B S Jacobson ◽  
D Branton
Keyword(s):  
Adenosine Triphosphatase ◽  
Wheat Germ ◽  
Plasma Membranes ◽  
Cell Attachment ◽  
Isolation Procedure ◽  
Chemical Analyses ◽  
Isolation Techniques ◽  
Cell Plasma ◽  
Membrane Bound ◽  
Membrane Isolation

HeLa cell plasma membranes have been purified after binding cells to polylysine-coated polyacrylamide beads. Cell attachment to beads and membrane recovery were maximal in a sucrose-acetate buffer, pH 5.0, at 25 degrees C. Measurements of ouabain-sensitive NaK-adenosine triphosphatase, membrane-bound 125I-wheat germ agglutinin, and chemical analyses showed that membranes on beads were of comparable or greater purity than membranes isolated by conventional methods. Because the isolation procedure is rapid (approximately 2.5 h), and produces membranes whose protoplasmic surfaces are fully exposed, it should be a useful supplement to standard isolation techniques.

A comparison of membrane-bound enzymes of the isolated brush border plasma membranes of the cestodes Hymenolepis diminuta and H. microstoma

Parasitology ◽  
1982 ◽  
Vol 84 (2) ◽  
pp. 391-396 ◽  
Author(s):  
P. W. Pappas ◽  
Elizabeth M. Narcisi
Keyword(s):  
Brush Border ◽  
Adenosine Triphosphatase ◽  
Plasma Membranes ◽  
Leucine Aminopeptidase ◽  
Enzymatic Activities ◽  
Hymenolepis Diminuta ◽  
Type I ◽  
Type Ii ◽  
Membrane Bound ◽  
Membrane Bound Enzymes

SUMMARYPreparations of isolated brush border plasma membrane of Hymenolepis diminuta and H. microstoma possess the following enzymatic activities: alkaline phosphohydrolase (E.C. 3.1.3.1); Type I phosphodiesterase (E.C. 3.1.4.1); ribonuclease (E.C. 3.1.4.22); adenosine triphosphatase (E.C. 3.6.1.3); and 5′-nucleotidase (E.C. 3.1.3.5). The following enzymatic activities could not be demonstrated in either membrane preparation: Type II phosphodiesterase (E.C. 3.1.4.18); cyclic adenosine-3′, 5′-monophosphate phosphodiesterase (E.C. 3.1.4.17); leucine aminopeptidase (E.C. 3.4.11.1); maltase (α-glucosidase; E.C. 3.2.1.20); and lactase (β-galactosidase; E.C. 3.2.1.23). These data generally agree with those of previous studies in which similar membrane-bound enzymes were demonstrated in intact (living) worms.

scholarly journals The induction of secondary cytolytic T lymphocytes by solubilized membrane proteins.

1978 ◽  
Vol 147 (3) ◽  
pp. 946-951 ◽  
Author(s):  
M Mescher ◽  
L Sherman ◽  
F Lemonnier ◽  
S Burakoff
Keyword(s):  
Plasma Membranes ◽  
Active Form ◽  
Protein A ◽  
Gel Filtration ◽  
Biologically Active ◽  
Cytolytic T Lymphocytes ◽  
Histocompatibility Complex ◽  
Cell Plasma ◽  
Immunological Specificity ◽  
Membrane Bound

Membrane-bound antigens responsible for induction of a secondary allogeneic murine cytolytic T-cell (CTL) response have been obtained in a soluble, biologically active form by deoxycholate solubilization of tumor cell plasma membranes. The active proteins are soluble by the criteria of both ultracentrifugation and gel filtration. The immunological specificity of the induced CTL and removal of the activity from solution by treatment with B6 anti-P815 (anti-H-2d) antiserum and Protein A-Sepharose demonstrate that the CTL-inducing activity is dependent upon solubilized major histocompatibility complex antigens.

scholarly journals A method for determining the adenosine triphosphatase content of energy-transducing membranes. reaction of 4-chloro-7-nitrobenzofurazan with the adenosine triphosphatase of bovine heart submitochondrial particles

1976 ◽  
Vol 159 (2) ◽  
pp. 347-353 ◽  
Author(s):  
S J Ferguson ◽  
W J Lloyd ◽  
G K Radda
Keyword(s):  
Mitochondrial Membrane ◽  
Adenosine Triphosphatase ◽  
Plasma Membranes ◽  
Single Amino Acid ◽  
Mitochondrial Atpase ◽  
Inner Mitochondrial Membrane ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Single Amino Acid Residue ◽  
Membrane Bound

1. Modification of a single amino acid residue by introduction of the nitrobenzofurazan group inactivates mitochondrial ATPase (adenosine triphosphatase) when membrane-bound in submitochondrial particles. The similarity between the reactions of both membrane-bound and isolated ATPase with 4-chloro-7-nitrobenzofurazan indicates that the single essential tryosine residue identified in the isolated enzyme [Ferguson, Loyd, Lyons & Radda (1975) Eur. J. Biochem. 54, 117-126] Is also a feature of the membrane-bound ATPase. 2. A procedure is presented for estimating the ATPase content of the inner mitochondrial membrane. It is based on the specificity of the incorporation of the nitrobenzofurazan group, and the ready removal of this group by compounds that contain a thiol group. This method indicates that 8.5% of the membrane protein is ATPase. The procedure should be applicable to the titration of the energy-transducing ATPases of bacterial plasma membranes and of the thylakoid membranes of chloroplasts. 3. Combination of the data obtained on the ATPase content of the bovine heart inner mitochondrial membrane with a titration of the cytochrome bc1 complex with antimycin indicates that these two components of the membrane are present in approximately equal amounts.

scholarly journals Integrins: An Important Link between Angiogenesis, Inflammation and Eye Diseases

Cells ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1703
Author(s):  
Małgorzata Mrugacz ◽  
Anna Bryl ◽  
Mariusz Falkowski ◽  
Katarzyna Zorena
Keyword(s):  
Cell Adhesion ◽  
Tissue Repair ◽  
Normal Development ◽  
Cell Attachment ◽  
Biological Activities ◽  
Integrin Receptors ◽  
Cytokine Activation ◽  
Eye Disorders ◽  
Membrane Bound ◽  
Cell To Cell Adhesion

Integrins belong to a group of cell adhesion molecules (CAMs) which is a large group of membrane-bound proteins. They are responsible for cell attachment to the extracellular matrix (ECM) and signal transduction from the ECM to the cells. Integrins take part in many other biological activities, such as extravasation, cell-to-cell adhesion, migration, cytokine activation and release, and act as receptors for some viruses, including severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2). They play a pivotal role in cell proliferation, migration, apoptosis, tissue repair and are involved in the processes that are crucial to infection, inflammation and angiogenesis. Integrins have an important part in normal development and tissue homeostasis, and also in the development of pathological processes in the eye. This review presents the available evidence from human and animal research into integrin structure, classification, function and their role in inflammation, infection and angiogenesis in ocular diseases. Integrin receptors and ligands are clinically interesting and may be promising as new therapeutic targets in the treatment of some eye disorders.

scholarly journals Insulin-induced rapid decrease of a major protein in fat cell plasma membranes.

1984 ◽  
Vol 259 (19) ◽  
pp. 12112-12116
Author(s):  
E J Schoenle ◽  
L D Adams ◽  
D W Sammons
Keyword(s):  
Plasma Membranes ◽  
Rapid Decrease ◽  
Major Protein ◽  
Fat Cell ◽  
Cell Plasma
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