Subharmonic bifurcation and chaos in a periodically modulated Co:MgF2 laser.
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Biomedical subjects
Publications and source records attributed to P Maly.
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Differences in frequency of postmyelographic adverse reactions were analyzed with respect to sex and age in a prospective study including 1026 patients injected with metrizamide and 739 injected with iohexol. Regardless of the type of contrast medium or myelography, all types of adverse reactions were 1.4-3.8 times as frequent in women as in men. Most of the differences were statistically significant. Headache was more frequent, while vomiting and dizziness were less frequent in both women and men aged 26-50 years compared with those over 50 years of age. Dizziness and increased low back pain were consistently reported spontaneously by the patients less frequently than emerged via formal interview. The large differences between the sexes suggest that further research on contrast media toxicity would be best performed with separation of the data by gender.
The accuracy of duplex-scanning and angiography in detecting ulceration in the carotid arteries was evaluated. Sixty-nine patients underwent duplex-scanning and carotid arteriography, and the findings were blindly compared to the operative specimens. Duplex-scanning had a significantly higher sensitivity (90 vs 48%, P less than 0.001) and accuracy (88 vs 59%, P less than 0.001) than angiography. There was no difference in specificity (84 vs 89%, P = 0.28). Comparison was also made between conventional arch angiography and selective carotid angiography in detecting ulceration. There was no significant difference between the methods (sensitivity 47 vs 50%, specificity 82 vs 100%). Finally, interobserver variability in detecting ulceration with duplex-scanning was evaluated in double-blind evaluation of the duplex-scans. The interobserver agreement was 84%. Duplex-scanning seems to be superior to angiography in detecting ulcerations in the extracranial carotid artery.
Four mandibular specimens were radiographically examined bilaterally to locate the mandibular canal. The following radiographic techniques were used: periapical and panoramic radiography, hypocycloidal tomography, and computed tomography (CT). The distance from the crest of the alveolar process to the superior border of the mandibular canal was measured in millimeters on all radiographs. The specimens were then sectioned, and the location of the mandibular canal (as measured on contact radiographs of the sections) was compared with measurements made on the other radiographs. The results showed that CT gave the most accurate position of the mandibular canal and is therefore probably the best method for preoperative planning of the implant surgery involving the area close to the mandibular canal.
Human serum and urine contain polypeptides which bind mannose 6-phosphate (M6P) and insulin-like growth factor II (IGF II) and crossreact with antibodies against the M6P/IGF II receptor. These polypeptides are considered to be fragments of the M6P/IGF II receptor. The major Mr approx. 205,000 fragment in serum and urine is about 10 kDa smaller in size than the membrane-associated receptor and is accompanied by minor forms with Mr values ranging from 104,000 to 180,000. The presence of receptor fragments in biological fluids indicates that shedding is one of the mechanisms contributing to the turnover of the M6P/IGF II receptor and that receptor fragments are part of the heterogenous group of serum proteins whic bind IGF II.
The surface topography of IGF I(insulin-like growth factor I) was investigated by chemical modification of amino acid residues in free IGF I and bound to type I IGF receptor or to monoclonal antibody MAB43. Tyrosine residues were modified either by chloramine-T or lactoperoxidase catalyzed iodination. In the free IGF I molecule, all 3 tyrosine residues, A19 (Tyr-60), B25 (Tyr-24), and C2 (Tyr-31), were iodinated. Monoclonal antibody MAB43 protected IGF I against modification at tyrosine residue A19, and in the type I IGF receptor-IGF I complex, all 3 tyrosine residues were shielded against iodine incorporation. These results allow the prediction of the binding domains in the IGF I molecule. The minimal receptor binding site in IGF I would include amino acid residues B25 to C2 and, possibly, the C-terminal part of the A-domain with tyrosine residue A19.
Pentamannosyl phosphate substituted bovine serum albumin (PMP-BSA) and insulin like growth factor II (IGF II) bind specifically to immobilized mannose 6-phosphate/insulin like growth factor II receptor. An excess of IGF II inhibited binding of PMP-BSA by less than or equal to 20%, and an excess of PMP-BSA inhibited binding of IGF II by less than or equal to 10%. Polyclonal antibodies against the receptor purified from human liver inhibited preferentially the binding of PMP-BSA, and a monocloncal antibody 2C2 inhibited only the binding of IGF II to the receptor. Similar results were obtained for binding of PMP-BSA and IGF II to human skin fibroblasts. These results suggest that the binding sites for mannose 6-phosphate and IGF II reside in different portions of the receptor.
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A parallel, double-blind, randomized study comparing iohexol and metrizamide--both 180 mg l/ml--in lumbar myelography was carried out in 60 consecutive patients. Eight to 15 ml of contrast medium were administered with the upper level at the middle thoracic column. A detailed neurologic examination was performed before and 24 hr after myelography. EEG recordings--evaluated visually and with fast Fourier transformation analysis--and somatosensory evoked responses were registered before, 6 hr after, and 24 hr after myelography. All patients were observed for adverse reactions for 24-48 hr. Iohexol did not produce any epileptiform activity but epileptiform activity was detected in five patients receiving metrizamide. Iohexol produced significantly less frequent and less severe EEG changes than did metrizamide both at visual evaluation (p less than .0025) and at fast Fourier transformation analysis (p less than .04). No significant changes occurred in the early components of the somatosensory evoked potentials after either contrast medium. Iohexol caused significantly (p less than .002) less frequent and less severe adverse reactions than did metrizamide. The neurologic examination revealed no changes of clinical importance with either contrast agent.
The binding affinities of type I IGF receptor, purified to near homogeneity from human placental membranes, were characterized. For this receptor preparation, free of type II IGF receptor and essentially free of insulin receptor, dissociation constants of Kd = 0.05 nM for IGF I and of Kd = 0.2 nM for IGF II (linear Scatchard plots) were determined. Competitive binding studies indicated a cross-reactivity of approximately 40% for IGF II to the type I IGF receptor.
The type I IGF receptor from human placental membranes was purified to near homogeneity by affinity chromatography on IGF I-Sepharose. SDS-polyacrylamide gel electrophoresis of the affinity purified type I IGF receptor demonstrated a high molecular weight protein with Mr greater than or equal to 300,000 under non-reducing conditions. After reduction with 2-mercaptoethanol two protein bands were found of Mr = 125,000 and 95,000, representing the alpha- and beta-subunits of the receptor molecule, respectively. A co-purification of the insulin receptor through the IGF I-affinity column could be avoided by a preincubation step with insulin.
Ribosomal protein L11 is one of only two ribosomal proteins significantly iodinated when Escherichia coli 50 S subunits are modified by immobilized lactoperoxidase, and the major target has been shown previously to be tyrosine at position 7 in the N-terminal domain. This modification reduces in vitro termination activity with release factor (RF)-1 by 70-90%, but RF-2 activity is less affected (30-50%). The loss of activity parallels incorporation of iodine into the subunit. The 50 S subunits from L11-lacking strains of bacteria have highly elevated activity with RF-2 and low activity with RF-1. The iodination does not affect RF-2 activity but reduces the RF-1 activity further. Ribosomal proteins, L2, L6, and L25, are significantly labeled in L11-lacking ribosomes in contrast to the control 50 S subunits. L11 has been modified in isolation and incorporated back efficiently into L11-lacking ribosomes. This L11, iodinated also predominantly at Tyr 7, is unable to restore RF-1 activity to L11-lacking ribosomes in contrast to mock-iodinated protein. These results suggest the involvement of the N terminus of L11 in the binding domain of the bacterial release factors and indicate that there are subtle differences in how the two factors interact with the ribosome.
Treatment of E. coli ribosomal subunits with 2-iminothiolane coupled with mild ultraviolet irradiation leads to the formation of a large number of RNA-protein cross-links. In the case of the 30S subunit, a number of sites on 16S RNA that are cross-linked to proteins S7 and S8 by this procedure have already been identified (see ref. 6). Here, by using new or modified techniques for the partial digestion of the RNA and the subsequent isolation of the cross-linked RNA-protein complexes, three new iminothiolane cross-links have been localized: Protein S17 is cross-linked to the 16S RNA within an oligonucleotide encompassing positions 629-633, and protein S21 is cross-linked to two sites within oligonucleotides encompassing positions 723-724 and positions 1531-1542 (the 3'-end of the 16S RNA).
Equimolar doses of iohexol and metrizamide (0.48 mmol/kg body weight = 185 mg I/kg), administered in solutions iso- and hyperosmolar to the CSF, were injected subarachnoidally into rabbits under pentobarbital anaesthesia. No excitative effects of iohexol were observed in the behaviour of the rabbits during a 3-h period immediately after the injection. Metrizamide caused significant, severe excitative effects, ranging from hyperexcitability to repeated generalized seizures. The frequency and severity of excitative effects were independent of the osmolality of the metrizamide solutions injected.
During a 14-day period, 45 of 78 rabbits were treated intravenously with chlorpromazine (5 mg kg-1 day-1). Metrizamide or iohexol was injected subarachnoidally and the neurotoxic effects of each substance on rabbit behaviour were evaluated for 3 h in both chlorpromazine-treated and non-treated rabbits. Chlorpromazine increased both the excitative and the depressive effects of metrizamide and the depressive effects of iohexol. No signs of excitation were observed in chlorpromazine-treated and non-treated rabbits after subarachnoid injections of iohexol. In spite of a free flow of clear fluid from the needle both before and after the intended subarachnoid injection, radiography disclosed that 26 of 67 suboccipital injections inadvertently resulted in a subdural deposition of the contrast medium. Contrast medium effects following subdural injection significantly differed from those following subarachnoid injection.
Forty anaesthetized rabbits were injected subarachnoidally with equimolal doses, 0.48 mmol/kg body weight (= 185 mg I/kg), of iohexol and metrizamide, administered in solutions iso- and hyperosmolal to the CSF. Concentrations of Na, K, Ca and Mg in the CSF were determined before and 3 hours after the contrast medium injections. Iso-osmolal iohexol caused a uniform decrease in all four cations, which was believed to be a simple dilution. The hyperosmolal solution of iohexol caused a significant relative increase in Ca compared with Na, K and Mg. Both metrizamide solutions caused an increase in Ca over its pre-injection level and a significant relative increase of both Ca and Mg as compared with Na and K. The changes caused by the three latter solutions were consistent with an increase in the blood-brain barrier permeability.
The complete range of published sequences for ribosomal RNA (or rDNA), totalling well over 50,000 bases, has been used to derive refined models for the secondary structures of both 16S and 23S RNA from E. coli. Particular attention has been paid to resolving the differences between the various published secondary structures for these molecules. The structures are described in terms of 133 helical regions (45 for 16S RNA and 88 for 23S RNA). Of these, approximately 20 are still tentative or unconfirmed. A further 20 represent helical regions which definitely exist, but where the detailed base-pairing is still open to discussion. Over 90 of the helical regions are however now precisely established, at least to within one or two base pairs.
Further to our studies on the Escherichia coli 30S ribosomal subunit, the detailed surface topography of both 50S subunits and 70S ribosomes has been investigated by using iodination catalyzed by immobilized lactoperoxidase as the surface probe. In the 50S subunit, only proteins L2, L5, L10, and L11 were iodinated to a significant and reproducible extent. The targets of iodination were identified, after isolation of the individual iodinated proteins, and were as follows: in protein L2 (271 amino acids), tyrosine-102 and -160; in protein L5 (178 amino acids), tyrosine-142; in protein L10 (165 amino acids), tyrosine-132; in protein L11 (142 amino acids), tyrosine-7 and -61. In the 70S ribosome, only protein L5 was still iodinated to a significant extent from the 50S subunit, whereas in the 30S subunit the same spectrum of iodinated proteins was observed as that from iodinated isolated 30S subunits, with the exception that S21 was no longer present.