On the ultrastructure of the plasma membrane as determined by the electron microscope

Hillier, James; Hoffman, Joseph F.

doi:10.1002/jcp.1030420205

Cited by 127 publications

(26 citation statements)

References 25 publications

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“…To confirm that the mutations did not affect heme binding, recombinant NEAT domains expressed overnight were assayed for their ability to co-purify with endogenous heme during expression in E. coli. Each NEAT domain was purified as stated under "Experimental Procedures," and bound heme was detected by measuring the Soret absorbance at ϳ400 nm, a well documented spectroscopic assay used to detect the presence of bound heme iron (7,12,20,24,(35)(36)(37)(38)(39)(40). As indicated in Fig.…”

Section: Identification Of Functional Residuesmentioning

confidence: 99%

The Near-iron Transporter (NEAT) Domains of the Anthrax Hemophore IsdX2 Require a Critical Glutamine to Extract Heme from Methemoglobin

Honsa

Owens

Goulding

et al. 2013

Journal of Biological Chemistry

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Section: Identification Of Functional Residuesmentioning

confidence: 99%

The Near-iron Transporter (NEAT) Domains of the Anthrax Hemophore IsdX2 Require a Critical Glutamine to Extract Heme from Methemoglobin

Honsa

Owens

Goulding

et al. 2013

Journal of Biological Chemistry

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“…Katchalsky, Danon, and Nevo (1959) used a similar technique in a study of h u m a n erythrocytes, a n d assumed that the thin dense line at the surface of the cell represented the cell m e m b r a n e ; in their cells this line was about 60 A thick, in good agreement with our value of 55 A for r a b b i t red cells. Hillier a n d Hoffman (1953) estimated that the membranes…”

Section: Figure 1~mentioning

confidence: 99%

Studies on the Mode of Action of Excess of Vitamin A

Glauert

Daniel

Lucy

et al. 1963

The Journal of Cell Biology

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Rabbit erythrocytes have been haemolysed by treatment with vitamin A alcohol and the sequence of changes in the fine structure of the cells during lysis has been investigated by phase contrast microscopy of intact cells and electron microscopy of thin sections. The initial effect of the vitamin, which occurs within 1 minute, is the production of cells of bizarre appearance which have a greatly increased surface area relative to untreated cells. Large indentations appear in the surfaces of the cells, and vacuoles are formed from the indentations by a process that resembles micropinocytosis. The cells then become spherical and loss of haemoglobin begins as breaks appear in the membranes of some cells; finally, ghosts are produced that are no longer spherical but still contain numerous vacuoles. These observations support the thesis that one site of action of vitamin A is at lipoprotein membranes.

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“…The use of purified fractions also demonstrates a very great affinity of the phosphatide and protein fractions of the lipoprotein for protamine but does not enable us to specify which of these moieties might be the binding site in the whole cell. Such affinity would be followed by electrostatic alteration and possibly aggregation of the key structural elements, fibrils and lipid plaques, which would distort their regular arrangement and their normal permeability (15). Previous workers have demonstrated the affinity of lipoproteins for basic proteins and for other charged molecules and the inhibitory effects thus produced (16,17).…”

Section: Discussionmentioning

confidence: 99%

Studies on the Hemolytic Properties of Protamine

Becker

1961

The Journal of General Physiology

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A B S T R A (3 T The basic protein protamine causes a rapid hemolysis when incubated with the red blood cells of many mammalian species. The age of the cells does not affect the process. Neutralization of the active side groups of the protamine molecule with formalinization demonstrates that a specific degree of charge is necessary for hemolysis, as more than 30 per cent of the guanidine groups must remain unreacted to maintain activity. Unlike the hemolysis induced by the synthetic polypeptides polylysine and polyhomoarginine, protamine hemolysis is temperature-dependent.Whole lipoprotein material derived from red blood cell membranes inhibits protamine hemolysis to a greater extent than do the membranes themselves, serum, serum protein fractions, or cholesterol. The phosphatide and protein moieties derived from the membranes are quite avid in inhibiting protamine hemolysis. A probable explanation is that intracellular aggregation of these structural elements may cause changes in electrostatic charge and surface tension which result in increased permeability.The hemolytic and antitumor cell properties of protamine could not be segregated from its animal toxicity. Despite formalinization to a degree which eliminated the former, the compound remained quite toxic to mice and rabbits.Protamine is a basic protein with a molecular weight of approximately 4000 to 5000 which is separated by salt fraction (1) from its complex with desoxyribonucleic acid in the sperm heads of fish. It is composed of a linear aggregation of amino acids and contains a large percentage of arginine.It has been previously demonstrated that protamine is capable of inhibiting protein synthesis in ascites tumor cells following its uptake and combination with the cellular nucleic acids (2). Damage to the tumor cell membrane was minimal and the process was temperature-dependent. Protamine is also capable of producing hemolysis in vitro and this hemolytic effect may represent a factor in its animal toxicity or another mechanism of cellular damage. In view of the ability of protamine to penetrate cell membranes (2, 3) it appeared possible that its lysis of red blood cells might result from intracellu-433

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On the ultrastructure of the plasma membrane as determined by the electron microscope

Cited by 127 publications

References 25 publications

The Near-iron Transporter (NEAT) Domains of the Anthrax Hemophore IsdX2 Require a Critical Glutamine to Extract Heme from Methemoglobin

The Near-iron Transporter (NEAT) Domains of the Anthrax Hemophore IsdX2 Require a Critical Glutamine to Extract Heme from Methemoglobin

Studies on the Mode of Action of Excess of Vitamin A

Studies on the Hemolytic Properties of Protamine

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