scholarly journals ASSOCIATION OF H-2 ANTIGENS WITH THE CELL MEMBRANE FRACTION OF MOUSE LIVER

1961 ◽  
Vol 47 (6) ◽  
pp. 762-767 ◽  
Author(s):  
L. A. Herzenberg ◽  
L. A. Herzenberg
Keyword(s):  
Cell Membrane ◽  
Membrane Fraction ◽  
Mouse Liver

[3H]5-HT binding sites and 5-HT-sensitive adenylate cyclase in glial cell membrane fraction

1980 ◽  
Vol 198 (2) ◽  
pp. 361-374 ◽  
Author(s):  
G. Fillion ◽  
D. Beaudoin ◽  
J.C. Rousselle ◽  
J. Jacob
Keyword(s):  
Cell Membrane ◽  
Adenylate Cyclase ◽  
Glial Cell ◽  
Binding Sites ◽  
Membrane Fraction

scholarly journals STUDIES ON THE FUNCTION OF CELL MEMBRANE 3rdREPORT:ON THE PURITY OF LIVER CELL MEMBRANE FRACTION ISOLATED FROM CCl4-TREATED RATS

1973 ◽  
Vol 23 (5) ◽  
pp. 639-644 ◽  
Author(s):  
Masato KUCHII ◽  
Yasusuke MASUDA ◽  
Nobuyuki OKADA ◽  
Hiroyuki YAMAMOTO ◽  
Tadashi MURANO
Keyword(s):  
Cell Membrane ◽  
Liver Cell ◽  
Membrane Fraction ◽  
Liver Cell Membrane

scholarly journals Inhibition of DNA synthesis at the hemimethylated pBR322 origin of replication by a cell membrane fraction

1992 ◽  
Vol 20 (1) ◽  
pp. 105-109 ◽  
Author(s):  
Abderrahim Malki ◽  
Renée Kern ◽  
Masamichi Kohiyama ◽  
Patrick Hughes
Keyword(s):  
Cell Membrane ◽  
Dna Synthesis ◽  
Membrane Fraction ◽  
Origin Of Replication ◽  
A Cell ◽  
Inhibition Of Dna Synthesis

scholarly journals Subcellular localization of NAD(P)H oxidase(s) in human neutrophilic polymorphonuclear leucocytes

1978 ◽  
Vol 176 (1) ◽  
pp. 175-178 ◽  
Author(s):  
D B Iverson ◽  
P Wang-Iverson ◽  
J K Spitznagel ◽  
L R DeChatelet
Keyword(s):  
Cell Membrane ◽  
Nadph Oxidase ◽  
Subcellular Localization ◽  
Density Gradient ◽  
Membrane Fraction ◽  
Sucrose Density Gradient ◽  
Human Neutrophils ◽  
Polymorphonuclear Leucocytes

NADH and NADPH oxidase activities in a homogenate of human neutrophils co-sediment in a linear sucrose density gradient under either velocity or isopycnic conditions of centrifugation. The position of these activities in the gradient does not correspond to any known subcellular granule or to the cell-membrane fraction. These data suggest that the oxidase activities may reside in a unique granule that has previously not been recognized.

scholarly journals Localization of the nuclear receptor CAR at the cell membrane of mouse liver

FEBS Letters ◽  
2005 ◽  
Vol 579 (30) ◽  
pp. 6733-6736 ◽  
Author(s):  
Chika Koike ◽  
Rick Moore ◽  
Masahiko Negishi
Keyword(s):  
Cell Membrane ◽  
Nuclear Receptor ◽  
Mouse Liver

scholarly journals Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia.

1986 ◽  
Vol 103 (3) ◽  
pp. 755-766 ◽  
Author(s):  
B R Stevenson ◽  
J D Siliciano ◽  
M S Mooseker ◽  
D A Goodenough
Keyword(s):  
Molecular Weight ◽  
Tight Junction ◽  
Membrane Fraction ◽  
Mouse Liver ◽  
Immunofluorescent Staining ◽  
Junctional Complex ◽  
Madin Darby Canine Kidney ◽  
Complex Region ◽  
Darby Canine Kidney ◽  
Canine Kidney

A tight junction-enriched membrane fraction has been used as immunogen to generate a monoclonal antiserum specific for this intercellular junction. Hybridomas were screened for their ability to both react on an immunoblot and localize to the junctional complex region on frozen sections of unfixed mouse liver. A stable hybridoma line has been isolated that secretes an antibody (R26.4C) that localizes in thin section images of isolated mouse liver plasma membranes to the points of membrane contact at the tight junction. This antibody recognizes a polypeptide of approximately 225,000 D, detectable in whole liver homogenates as well as in the tight junction-enriched membrane fraction. R26.4C localizes to the junctional complex region of a number of other epithelia, including colon, kidney, and testis, and to arterial endothelium, as assayed by immunofluorescent staining of cryostat sections of whole tissue. This antibody also stains the junctional complex region in confluent monolayers of the Madin-Darby canine kidney epithelial cell line. Immunoblot analysis of Madin-Darby canine kidney cells demonstrates the presence of a polypeptide similar in molecular weight to that detected in liver, suggesting that this protein is potentially a ubiquitous component of all mammalian tight junctions. The 225-kD tight junction-associated polypeptide is termed "ZO-1."

LOCATION OF PROTEINASE IN CELLS OF A SPECIES OF MICROCOCCUS

1962 ◽  
Vol 8 (5) ◽  
pp. 785-794 ◽  
Author(s):  
I. J. McDonald
Keyword(s):  
Sodium Chloride ◽  
Cell Membrane ◽  
Yeast Extract ◽  
Membrane Fraction ◽  
Culture Supernatant ◽  
Cytoplasmic Membrane ◽  
Cell Envelope ◽  
Sonic Treatment ◽  
Added Salt ◽  
In Cells

Micrococcus sp. (ATCC No. 407) grown in tryptone yeast extract broth produced proteinase active against casein. In broth containing 2.0% sodium chloride, about 90% of the proteinase was in the culture supernatant; in broth without added salt, about 66% was associated with the cells. When such cells were washed with 2% sodium chloride, about one-half the associated proteinase was released. Presumably this saline-extractable portion of the proteinase is loosely held at the ceil surface, possibly by ionic linkages. A further yield of proteinase could be obtained from saline-washed cells by treatments that ruptured the cells or altered the permeability of the cell membrane. This so-called bound proteinase became accessible to the substrate, but was not liberated into the suspending medium on lysozyme treatment of saline-washed cells. When lysozyme-treated cells were fractionated, the proteinase was found with the cytoplasmic membrane fraction. During sonic treatment of saline-washed cells, the bound. proteinase was released without appreciable disintegration of the cell envelope suggesting that it may not be an integral part of the cell membrane.

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