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M Rytel

Publications and source records attributed to M Rytel.

13 recordsLinked to original sources

Accuracy in tunnel placement for ACL reconstruction. Comparison of traditional arthroscopic and computer-assisted navigation techniques.

The purpose of this randomized, prospective study was to compare accuracy in tunnel placement as performed with a traditional arthroscopic anterior cruciate ligament (ACL) reconstruction technique and with KneeNavTM ACL, a computer-assisted surgical navigation technique. Two surgeons experienced in ACL reconstruction, but inexperienced in computer-assisted surgical navigation technique, each randomly used traditional arthroscopic guides or KneeNavTM ACL to drill a tunnel in twenty identical foam knees. Placement of the resulting tibial and femoral tunnels was measured with a computer-assisted digitizing method and compared to traditional biplanar radiographs. Statistical analysis with Student's t-test was used to compare the distance from the ideal tunnel placement to the femoral and tibial tunnels. Accuracy of tunnel placement with KneeNavTM ACL was significantly better than that obtained with the traditional arthroscopic technique. Distances from the ideal tunnel placement to the femoral and tibial tunnels were 4.2 +/- 1.8 mm (mean +/- SD) and 4.9 +/- 2.3 mm, respectively, for the traditional arthroscopic technique, and 2.7 +/- 1.9 mm (femur) and 3.4 +/- 2.3 mm (tibia) for KneeNavTM ACL. These differences were statistically different. Tunnel placement for ACL reconstruction with KneeNavTM ACL, an image-based, computer-assisted surgical navigation device with a simple and intuitive interface, was more accurate than with the traditional arthroscopic technique.

Anterior Cruciate Ligament↗

The 3A Band System in the Spectrum of the (13)C(16)O Molecule.

In the emission spectrum of the carbon monoxide (13)C(16)O isotopic molecule three bands comprising about 1820 lines of the 3A band system (c(3)Pi-a(3)Pi) were recorded and analyzed. The 0-0 and 0-1 bands of this system were photographed for the first time and the 0-2 band was rephotographed by using methods of conventional high-resolution spectroscopy. The result of the rotational band analysis includes expanding of the spectrum interpretation up to J = 25 as well as the identification of four previously unobserved branches P(13), R(13), P(31), and R(31). Because of strong perturbations in the c(3)Pi (v = 0) state, the calculation of the rovibronic structure constants was performed only for the lower a(3)Pi state. By using a calculation based on a nonlinear least-squares method, an effective Hamiltonian of Brown [J. M. Brown, E. A. Colbourn, J. K. G. Watson, and F. D. Wayne, J. Mol. Spectrosc. 74, 294-318 (1979)] and a separative procedure proposed by Curl-Dane-Watson [R. F. Curl and C. B. Dane, J. Mol. Spectrosc. 128, 406-412 (1988); J. K. G. Watson, J. Mol. Spectrosc. 138, 302-308 (1989)], it was possible to derive the rotational structure constants for the v = 0, 1, and 2 levels for the a(3)Pi state in the (13)C(16)O isotopic molecule. Term values for the c(3)Pi (v = 0) level and the equilibrium molecular constants for the a(3)Pi state also are reported. Copyright 1999 Academic Press.

Journal Article↗

Purification and characterization of nuclease I associated with rye germ ribosomes.

A nuclease has been purified about 100-fold from ammonium chloride wash of rye germ ribosomes. The enzyme was electrophoretically homogeneous. Its M, was 20,000 and pl 4.8. The neclease hydrolyzed endonuclelytically DNA and RNA and was accompanied by 3-nucleotidase activity. The enzyme degraded RNA to oligonucleotides with a phosphomonoester bond at position 5', and both denatured and native DNA to 5'-OH and 3'-phosphate-terminated fragments. Zinc ions and 2-mercaptoethanol stimulated deoxyribonucleolytic activity. EDTA, polyamines and heparin had only little or no effect. The enzyme is a glycoprotein containing 28% of carbohydrate which consists of fucose, mannose and glucosamine. The nuclease isolated is classified as nuclease I.

Carbohydrates↗

Aspergillus terreus infective endocarditis on a porcine heterograft valve.

We present the first reported case of Aspergillus endocarditis occurring on a porcine heterograft prosthesis and discuss the literature regarding both Aspergillus endocarditis and endocarditis on a porcine valve. A 65-year-old man underwent aortic valve replacement with a porcine heterograft. Several weeks later he exhibited signs of infection and then of valve failure. Upon removal, the porcine valve substance was found to be grossly infiltrated and destroyed by the Aspergillus organism. The porcine valve has an excellent reputation of being resistant to infection and relatively easy to sterilize by medical management alone. Several surveys attest to the low incidence of endocarditis. Because of our experience with the destruction caused by Aspergillus, however, and because antimicrobials generally fail to eradicate this organism, we urge prompt operation to remove the heterograft valve involved with infection by this organism. The valve diseased with Aspergillus should be replaced with a mechanical prosthesis. In the aortic position, extra-anatomic replacement should be considered to facilitate eradication of periannular infection postoperatively.

Aged↗

The presence of deoxyribonucleolytic activity in cytoplasmic ribosomes of rye (Secale cereale L) germs.

Deoxyribonucleolytic activity was found to be associated with cytoplasmic ribosomes and ribosomal subunits of rye germs. The activity has the pH optimum at 5.0. Treatment of ribosomes and 60S subunits with 0.5 M-ammonium chloride released a considerable part of deoxyribonucleolytic and ribonucleolytic activity; treatment of 40S subunits resulted in a complete release of deoxyribonucleolytic activity and partial release of ribonucleolytic activity. This suggests the presence in ribosomes of rye germs of two types of nucleolytic enzymes: an enzyme of the nuclease I type with deoxyribonuclease and ribonuclease activities, and typical ribonucleases hydrolysing RNA only.

Ammonium Chloride↗