Flexural rigidity of marginal bands isolated from erythrocytes of the newt
نویسندگان
چکیده
The marginal band is a bundle of microtubules residing at the periphery of nucleated erythrocytes of nonmammalian vertebrates and some invertebrates. Marginal bands from erythrocytes of the newt (Notopthalmus viridescens) were isolated from the cells as intact structures by treatment with detergent and either mild protease or high salt. Isolated bands were subjected to mechanical testing by stretching the band between a glass microhook and a calibrated glass fiber. The deflection of the fiber provided a measure of the force on the band. The flexural rigidity of the band was determined from measurements of the band deformation as a function of applied force. Bands isolated with either of two proteases (pepsin or elastase) or with high salt exhibited elastic behavior with a flexural rigidity of approximately 9.0 X 10(-12) dyn.cm2. Treatment of bands with chymopapain caused an increase in band rigidity and inelastic behavior. Estimates of the contribution of the band to cellular rigidity are made based on the measurements of the structural properties of the isolated band. The band provides the cell with a large resistance to indentations at the rim and to large extensions, while maintaining a high degree of flexibility in small extensions or flexure.
منابع مشابه
Flexural Rigidity of Marginal Bands Isolated from Erythrocytes of the Newt
The marginal band is a bundle of microtubules residing at the periphery of nucleated erythrocytes of nonmammalian vertebrates and some invertebrates. Marginal bands from erythrocytes of the newt (Notopthalmus viridescens) were isolated from the cells as intact structures by treatment with detergent and either mild protease or high salt. Isolated bands were subjected to mechanical testing by str...
متن کاملUltraviolet microbeam irradiation
Marginal bands were isolated from newt red blood cells and, using monochromatic light from an ultraviolet microbeam, the marginal band microtubules were irradiated in vitro to produce areas of reduced birefringence (ARBs). The ARBs neither moved nor changed shape after they were formed, though the marginal bands sometimes changed shape during the irradiation. Marginal band ARBs 'were regions in...
متن کاملElastic stability of columns with variable flexural rigidity under arbitrary axial load using the finite difference method
Abstract: In this paper, the finite difference method (FDM) is applied to investigate the stability analysis and buckling load of columns with variable flexural rigidity, different boundary conditions and subjected to variable axial loads. Between various mathematical techniques adopted to solve the equilibrium equation, the finite difference method, especially in its explicit formulat...
متن کاملTHE ISOLATION OF ENZYME TRANSKETOLASE FROM HUMAN ERYTHROCYTES: THE CHARACTERIZATION OF ITS QUARTERNARY STRUCTURE
Human erythrocyte transketolase (sedoheptulose-7-phosphate: D-glyceraldehyde-3-phosphate, glycolaldehyde transferase, E.C. 2.2.1.1.) has been isolated from erythrocytes with a specific activity of 59.84 U/mg. SDS-PAGE and SE-HPLC were used both as a measure of purity and as a preparative mean to obtain a higher degree of purity. Four protein bands corresponding to molecular weights of 32,0...
متن کاملThe cytoskeletal system of nucleated erythrocytes. II. presence of a high molecular weight calmodulin-binding protein
Calmodulin was detected in dogfish erythrocyte lysates by means of phosphodiesterase activation. Anucleate dogfish erythrocyte cytoskeletons bound calmodulin. Binding of calmodulin was calcium-dependent, concentration-dependent, and saturable. Cytoskeletons consisted of a marginal band of microtubules containing primarily tubulin, and trans-marginal band material containing actin and spectrinli...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of Cell Biology
دوره 108 شماره
صفحات -
تاریخ انتشار 1989