scholarly journals The Chemical Composition of Wool X. Material Digested by Trypsin From Fibres and Cortical Cells

1972 ◽  
Vol 25 (6) ◽  
pp. 1225 ◽  
Author(s):  
DE Peters ◽  
JH Bradbury
Keyword(s):  
Electron Microscopy ◽  
Chemical Composition ◽  
Cell Membrane ◽  
Formic Acid ◽  
Acid Treatment ◽  
Mechanical Agitation ◽  
Cortical Cells ◽  
Membrane Complex ◽  
Cell Membrane Complex

Samples of wool, wool pretreated with formic acid, and cortical cells produced by mechanical agitation in formic acid have been digested by trypsin. The evidence shows that the formic acid treatment is not degradative. It is found by electron microscopy that trypsin digests the endocuticle, part of the cell membrane complex, and the nuclear remnants and intermacrofibrillar material of the. cortex. These digested components amount to about 3�6, 1� 8, and 12�6% by weight of the fibre respectively.

scholarly journals The Chemical Composition of Wool V. The Epicuticle

1968 ◽  
Vol 21 (2) ◽  
pp. 375 ◽  
Author(s):  
NLR King ◽  
JH Bradbuby
Keyword(s):  
Electron Microscopy ◽  
Amino Acids ◽  
Amino Acid ◽  
Chemical Composition ◽  
Cell Membrane ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Lipid Content ◽  
Membrane Complex ◽  
Cell Membrane Complex

The cuticle membranes of wool raised by chlorine (epicuticle) and by bromine have been isolated and their thicknesses determined by electron microscopy of gold-shadowed specimens. These were found to be 32�10 A and 140�40 A respectively. The epicuticle consists of 78% protein, 5% lipid, 4% ash, and a negligible amount of carbohydrate. Amino acid analyses of the epicuticle and the dissolved protein which fills the Allworden sacs show that (with the exception of glycine) those amino acids which are present in larger amount in the epicuticle than in the whole cuticle are present in smaller amount in the dissolved protein and vice versa. Furthermore, the amino acid composition of the epicuticle resembles that of the cuticle more closely than that of the protein from the cell membrane complex. This fact, together with its low lipid content, suggests that it may not originate from the cuticle cell membrane complex.

scholarly journals The Chemical Composition of Wool XV. The Cell Membrane Complex

1976 ◽  
Vol 29 (2) ◽  
pp. 43 ◽  
Author(s):  
DE Peters ◽  
JH Bradbury
Keyword(s):  
Cell Membrane ◽  
Cross Sections ◽  
Performic Acid ◽  
Appreciable Amount ◽  
Lysine Content ◽  
Cortical Cells ◽  
Membrane Complex ◽  
Chemical Attack ◽  
Cross Links ◽  
Cell Membrane Complex

The cell membrane complex of wool has been examined by electron microscopy of stained. cross sections after immersion of the wool in formic acid. The cell membrane complex of the cortex is considerably modified by the treatment, but that of the cuticle appears unchanged. Resistant membranes from cuticle cells, cortical cells and wool have been prepared by treatment with performic acid-ammonia. Amino acid analyses show that the resistant membranes from the cuticle contain citrulline but those from cortical cells do not. It is concluded that the cell membrane complex of the cuticle differs from that of the cortex. Because of the high lysine content of the resistant membranes, their resistance to chemical attack, the hydrophobicity of epicuticle and the observation of a small amount of e-(y-glutamyl)lysine, it is postulated that the resistant membranes may contain an appreciable amount of e-(y-glutamyl)lysine cross links.

Role of Nonkeratinous Proteins in Crimp Formation of Wool Fibers by Draft and Immediate Relaxation

1988 ◽  
Vol 58 (1) ◽  
pp. 22-26 ◽  
Author(s):  
Ryo Umehara ◽  
Yutaka Shibata ◽  
Yoshihiko Masuda ◽  
Hiraku Ito ◽  
Takeaki Miyamoto ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Formic Acid ◽  
Relaxation Process ◽  
Proteolytic Enzyme ◽  
Membrane Complex ◽  
Wool Fibers ◽  
Cell Membrane Complex

The role of nonkeratinous proteins in the crimp formation of wool fibers by draft and immediate relaxation was investigated. For this purpose, Australian Shropshire wool fibers were treated with formic acid and pronase (proteolytic enzyme) to modify the nonkeratinous proteins. Formic acid is known to remove some of the intercellular cement, one of the nonkeratinous proteins, from the cell membrane complex, while pronase removes all nonkeratinous proteins. Little crimp formation occurred in the wool fibers treated with formic acid and pronase, indicating that the nonkeratinous proteins, especially the intercellular cement of the cell membrane complex, play an important role in the crimp formation of wool fibers by the draft and immediate relaxation process. A similar effect on crimp formation also occurred when the wool fibers were steamed in a relaxed state.

High-voltage Electron Microscopy and 3-D reconstruction of human hair fiber ultrastructure

1989 ◽  
Vol 47 ◽  
pp. 116-117
Author(s):  
L. Rudy ◽  
R. Sneath ◽  
M. Song
Keyword(s):  
Electron Microscopy ◽  
Cell Membrane ◽  
High Voltage ◽  
Human Hair ◽  
Three Dimensional ◽  
High Voltage Electron Microscopy ◽  
Membrane Complex ◽  
Voltage Electron ◽  
High Voltage Electron ◽  
Cell Membrane Complex

The basic morphology of the non-keratinous regions of human hair fibers was studied using both conventional and high voltage electron microscopy. The non-keratinous regions of hair include the endocuticle, the cell membrane complex, and the nuclear remnants of the cortex. By characterizing these regions more clearly, the mechanisms by which external influences affect the hair can be understood. The nuclear remnants are surrounded by a cell membrane complex. Since thin sectioning often causes artifacts in these fragile structures, a three-dimensional reconstruction using serial, semi-thick sections was completed to reveal their morphological nature.Human hair fibers collected from a female subject, had not been treated with any chemically active processes. One centimeter samples were collected near the scalp region of the back of the head. The fibers were embedded in Epon-812. Serial, semi-thick sections, 0.25u thick, were sectioned and collected on copper slot, formvar-coated grids. Post-staining was completed with uranyl acetate and lead citrate. Sections were examined in an AEl EM7 Mk 1.2MV HVEM at an accelerating voltage of 1.0 MV.

Characterisation of formic acid-derived cell membrane complex proteins from wool

1992 ◽  
Vol 20 (2) ◽  
pp. 90S-90S ◽  
Author(s):  
GEOFFREY P.P. MITCHELL ◽  
JOSEPH MIFSUD ◽  
DONALD E. RIVETT ◽  
ANTHONY K. ALLEN
Keyword(s):  
Cell Membrane ◽  
Formic Acid ◽  
Membrane Complex ◽  
Cell Membrane Complex

New Advances in the Internal Lipid Composition of Wool

1988 ◽  
Vol 58 (6) ◽  
pp. 338-342 ◽  
Author(s):  
B. Nogues ◽  
L. Coderch ◽  
R. Julia ◽  
P. Erra
Keyword(s):  
Cell Membrane ◽  
Organic Solvents ◽  
Lipid Composition ◽  
Bilayer Structure ◽  
Membrane Complex ◽  
Wool Fibers ◽  
Cell Membrane Complex

The presence of glycolipids on wool fibers has been detected by analyzing the solubilized material when wool is treated with different organic solvents selected to remove internal lipids. One of these has been isolated and identified as a glucosilceramide. These compounds are thought to contribute to the bilayer structure that may be present in the β-layers of the cell membrane complex.

scholarly journals Histochemical observation of the cell membrane complex of hair.

1992 ◽  
Vol 48 (8) ◽  
pp. 420-426 ◽  
Author(s):  
Sachio Naito ◽  
Toshie Takahashi ◽  
Michihiro Hattori ◽  
Kozo Arai
Keyword(s):  
Cell Membrane ◽  
Membrane Complex ◽  
Histochemical Observation ◽  
Cell Membrane Complex
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