Advances in protein chemistry. / Volume by M L Anson; John T Edsall

By M L Anson; John T Edsall

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Schmidt (1939, a) found that the extruded shafts show positive form birefringence, from which he suggeRts that the structure is essentially fibrous and that extrusion may be due to an elongation of previously folded chains. E M investigation of trichocyst structure has revealed a most interesting and unexpected structure (Schmitt, Hall, and Jakus, 1943). The extruded shaft behind the dense pointed tip (Fig. 3, a) shows a banded structure (Fig. 3, b) which extends to the tapered end. The distance between the bands is strikingly constant in the shafts emitted from any single cell and averages about 600-650 A.

Block (1938) later sponsored the view that newokeratin may not be in the sheath at all but rather in the neurofibrils. From the preceding section it is obvious that this view is untenable. Block agrees with Speakman and Townsend (1937), however, that the chemical properties of neurokeratin result from the customary treatment of brain with organic solventa. He states that a protein having amino acid composition similar to that of neurokeratin can be obtained by water extraction of ground brain. This fact does not necessarily exclude the possibility that neurokeratin ia a sheath protein.

Polarized light. . . . . X-ray diffraction. . . . Electron microscope. . . . VL. General Considerations of Protein Fibor Structme References . . . . . . . . . . . . . . . . . . 54 5,; 55 56 58 60 G1 . . . . . 61 61 . . . . 64 . . . . . Va . . . . . 63 INTRODUCTION Proteins antl coinplexes of proteins with lipids and ctlridiytlrit 1 ::s form the basis of the structural components of cells and tissue:;. Jl'ilf~r~ ;is these structural proteins have, in the past,, becn invcstigated chiefly by the techniques of classical morphology, advances during thc.

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