Studies on the succinylation of erythrocyte membranes

Moldow, Charles F.; Zucker‐Franklin, Dorothea; Gordon, Adrienne; Hospelhorn, Verne D.; Silber, Robert

doi:10.1016/0005-2736(72)90015-6

Cited by 17 publications

(4 citation statements)

References 33 publications

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“…Thus, we must accept that the observed increase in charge is insufficient and several hypothesis may be stated: (a) ionization of the grafted carboxyl group is not complete at pH 7 used for the measurement of electrophoretic mobility; (b) a partial reversibility of the reaction; but working at pH 3-4 during incubation times varying from 1 to 3 h, we cannot obtain this reversibility; (c) partial solubilization of membrane proteins produced by an increase of the overall negative charge. This fact has been reported by different authors when maleic and succinic anhydrides were used [8,16]; (d) the carboxyl groups are perhaps not all situated in the electrophoretic shear plane. Z-E isometry due to the ethylenic double bond, may explain that only 5()°/o of the grafted groups are electrophoretically active; (e) a last possibility would be the reaction of one molecule of citraconic anhyd ride with two amino groups.…”

Section: Discussionsupporting

confidence: 50%

Study of Amino Groups of the Human Platelet Membrane

Stoltz¹,

Nicolas²

1978

Acta Haematol

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The authors attempted to evaluate different reagents in order to quantify the amino groups of the platelet membrane. The study was carried out by the action of different aldehydes and acid anhydrides. The use of 2,4,6-trinitrobenzenesulfonic acid made possible an approach by electrophoresis and chemical assay. The results showed an increase in the surface charge corresponding to a mean number of amino groups varying from 1.86.10⁵ groups with citraconic acid to 3.94·10s groups with acetaldehyde.

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Section: Discussionsupporting

confidence: 50%

Study of Amino Groups of the Human Platelet Membrane

Stoltz¹,

Nicolas²

1978

Acta Haematol

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“…This was the chemical basis for classifying peripheral and integral membrane proteins. Another such example is in work presented by Moldow et al (24), who demonstrate succinylation of erythrocytes results in release of soluble proteins but does not release integral membrane proteins from their association with membrane. In retrospect, this result would seem intuitive since membrane proteins mask most of their charged amino acid side-chains through salt-linkages or unusual pK values.…”

Section: Outer and Inner Membrane Separationmentioning

confidence: 99%

Lateral diffusion in nuclear membranes.

Schindler¹,

Holland²,

Hogan³

1985

The Journal of Cell Biology

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Chemical modification of rat liver nuclei with citraconic anhydride selectively removed outer nuclear membrane. This conclusion was based on (a) transmission electron microscopy, (b) lipid analysis, (c) lamin B as an inner membrane-associated marker, and (d) the demonstration of phospholipid lateral mobility on outer membrane-depleted nuclei as a criteria for inner membrane integrity. Addition of urea or N-ethylmaleimide resulted in the additional disruption of inner membrane. Fluorescence photobleaching was used to determine the long range (>4/zm) lateral transport of lectin receptors and a phospholipid analog in both membranes. The diffusion coefficient for wheat germ agglutinin on whole nuclei was 3.9 x 10 -l° cm2/s whereas the diffusion coefficient for wheat germ agglutinin in outer membranedepleted nuclei was <10 -t2 cm2/s. Phospholipid mobilities were the same in whole and outer membrane-depleted nuclei (3.8 x 10 -9 cm2/s). The protein diffusion differences observed between whole and outer membrane-depleted nuclei may be interpreted in the context of two functionally different membrane systems that compose the double bilayer of the nucleus.The cell nucleus is encapsulated by two bilayer membranes that appear to converge at the periphery of pore complexes (1-3). The outer membrane (cytoplasmic) has been demonstrated to merge with endoplasmic reticulum (ER), ~ while biochemical evidence suggests that a number of ER enzymes may be present in the outer nuclear membrane (l, 2). The composition and nature of the inner nuclear membrane (nucleoplasmic) has for the most part remained a mystery. Morphologically, the inner nuclear membrane appears to be precipitated on a dense lamella or nucleo-cytoskeleton (2, 3). This superstructure is predominantly composed of a series of polypeptides, termed lamins, that form a well-organized polymeric network (4, 5). Evidence from Gerace and Blobel (5) suggest that a subgroup of lamins, lamin B, forms a tight association with the inner nuclear membrane that can be abrogated with Triton X-100. Although these two membranes would appear to be very different structurally, i.e., inner nuclear membrane attaches to a cytoskeletal structure, their separation and characterization has proven difficult. The two most widely used methods for nuclear membrane separation and isolation have been demonstrated to be ineffective (Triton X-I00; see reference 6) or chemically disruptive to membrane enzymes through acid denaturation (2.5% citric acid; see references 7 and 8). The evidence used to validate each ~Abbreviations used in this paper: Con A, concanavalin A; ER, endoplasmic reticulum; NBD-PE, N-4-nitrobenzo-2-oxa-l,3-diazole phosphatidylethanolarnine; TEM, transmission electron microscopy; WGA, wheat germ agglutinin. 1408procedure has been (a) electron microscopic analysis of inner and outer membrane, and (b) the presence of phospholipid in pelleting nuclear structures after separation treatment. By these previously used criteria and two others, the requirement of lamin B for inner ...

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“…When the electrostatic repulsive forces between complexes are increased by alkalinization or by the removal of divalent counterions, many membranes can be induced to undergo fragmentation into lipoprotein units br into smaller vesicular membranes. For example, the mitochondrial membrane can be disrupted by sonication at high pH [42] ; the halobacterium membrane is disrupted dramatically by dilution of the high salt medium [43] ; the red cell membrane is disrupted extensively by chelation of divalent metal ions with 5 mM EDTA [44] , succinylation of the proteins [45] and sonication at high pH [46] . These effects can all be prevented by cross-linking with glutaraldehyde, thereby introducing new and stable protein-protein interactions into the membrane [46].…”

Section: Complexes Are Associated Into Domainsmentioning

confidence: 99%