## Abstract Using the interaction of polyacrylic anhydride with uridine or __N__‐acetyl derivatives of adenosine, cytidine, and guanosine, the water‐soluble copolymers, polyacryloylnucleosides, were obtained. The acryloylnucleoside units to acrylic acid units ratio in the copolymer was usually abou
The structure of fibrin. An electron microscopic investigation
✍ Scribed by G. Conio; G. Dondero; C. Troglia; V. Trefiletti; E. Patrone
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 603 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
An electron microscopic investigation on the structure of fibrin is reported. Fibrin morphology was investigated in a wide variety of experimental conditions, and by carefully controlled staining procedures. Two main band patterns A (230‐Å‐spaced main dark bands) and B (230‐Å‐spaced main light bands) are observed for stained fibrin; it is shown that the former results from the superimposition of both positive and negative staining, and the latter is given by positive staining. By suitable denaturation experiments, it was found that the fiber is composed of a regular alternation of lose and dense regions along the axis.
We have assumed that the monomer of fibrin is described by the three‐nodular model of Hall and Slayter, as supported by recent investigations. The monomers are arrayed according to a head‐to‐tail sequence along the fiber, and to a staggered lateral association. This model accounts for all the experimental observations, and predicts well the high‐resolution band pattern of fibrin. It further agrees with the results of a recent work on the early stages of the fibrinogen‐to‐fibrin conversion.
📜 SIMILAR VOLUMES
qu'une telle observation requiert une technique a haute sensibilite. Enfin le caractitre stable de l'etat polygonis peut Btre clairement illustre par le fait queles monocristaux que nous avons examines ne recristallisent pas L l'etat solide.
## Abstract Earlier studies by the authors showed that the collagen fibrils in rat‐tail tendon have a bi‐modal distribution of fibril diameters from a time shortly after birth through to the onset of maturity at about 3–4 months. Present work has extended those observations for rats up to the age o