scholarly journals Morphological study of the integument and corporal skeletal muscles of two psammophilous members of Scincidae ( Scincus scincus and Eumeces schneideri )

2020 ◽  
Author(s):  
Jérôme Canei ◽  
Denis Nonclercq
2013 ◽  
Vol 12 (1) ◽  
pp. 52
Author(s):  
H. K. N. AL-Mhanna

Formalistic study elucidate that the larynx in the fourteen healthy indigenous male pigeons (Columba domestica) for benefit in the study of the respiratory physiology, histopathology, and the respiratory diseases analyzes. After bird's preparation, the larynx detected, and then the shape, position and its components studied in details.The larynx emerges in the caudal part of the oropharyngeal cavity as a heart-shaped cartilaginous mass. It composed of a single hyaline cricoid cartilage which consisted of body and left and right wings, double hyaline arytenoid cartilages which consisting of body and rostral and caudal processes, and single hyaline procricoid cartilage which consisted of body dorsally and curved tail caudoventrally. These cartilaginous components surrounded by laryngeal skeletal muscles intrinsic (superficial and deep) and extrinsic (rostral, caudolateral, and caudomedial).


Author(s):  
D. A. Fischman ◽  
J. E. Dennis ◽  
T. Obinata ◽  
H. Takano-Ohmuro

C-protein is a 150 kDa protein found within the A bands of all vertebrate cross-striated muscles. By immunoelectron microscopy, it has been demonstrated that C-protein is distributed along a series of 7-9 transverse stripes in the medial, cross-bridge bearing zone of each A band. This zone is now termed the C-zone of the sarcomere. Interest in this protein has been sparked by its striking distribution in the sarcomere: the transverse repeat between C-protein stripes is 43 nm, almost exactly 3 times the 14.3 nm axial repeat of myosin cross-bridges along the thick filaments. The precise packing of C-protein in the thick filament is still unknown. It is the only sarcomeric protein which binds to both myosin and actin, and the actin-binding is Ca-sensitive. In cardiac and slow, but not fast, skeletal muscles C-protein is phosphorylated. Amino acid composition suggests a protein of little or no αhelical content. Variant forms (isoforms) of C-protein have been identified in cardiac, slow and embryonic muscles.


Author(s):  
Susan B.G. Debaene ◽  
John S. Gardner ◽  
Phil S. Allen

The coleorhiza is a nonvascular sheath that encloses the embryonic radicle in Poaceae, and is generally the first tissue to emerge during germination. Delicate hairlike extensions develop from some coleorhiza cells prior to radicle emergence. Similar to root hairs, coleorhiza hairs are extremely sensitive to desiccation and are damaged by exposure to negative water potentials. The coleorhiza of Lolium perenne is somewhat spherical when first visible, after which a knob forms at a right angle to the caryopsis due to inner pressure from the elongating radicle. This knob increases in length until the radicle finally punctures the coleorhiza. Standard fixation procedures cause severe desiccation of coleorhiza cells and hairs, making morphological study of the coleorhiza difficult. This study was conducted to determine a more successful process for coleorhiza preservation.


Author(s):  
F.T. Llados ◽  
V. Krlho ◽  
G.D. Pappas

It Is known that Ca++ enters the muscle fiber at the junctional area during the action of the neurotransmitter, acetylcholine (ACh). Pappas and Rose demonstrated that following Intense stimulation, calcium deposits are found In the postsynaptic muscle membrane, Indicating the existence of calcium uptake In the postsynaptic area following ACh release. In addition to this calcium uptake, when mammal Ian skeletal muscles are exposed to a sustained action of the neurotransmitter, muscle damage develops. These same effects, l.e., Increased transmitter release, calcium uptake and finally muscle damage, can be obtained by Incubating the muscle with lonophore A23178.


1976 ◽  
Vol 14 (2) ◽  
pp. 123 ◽  
Author(s):  
Kye Heon Jeong ◽  
Han Jong Rim ◽  
He Young Yang ◽  
Woo Kap Kim ◽  
Chang Whan Kim

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