Biomedical subjects

A Lin

Publications and source records attributed to A Lin.

At least 55 records · Page 3Linked to original sources

PubMed1987

The primary structure of rat ribosomal protein S12. The relationship of rat S12 to other ribosomal proteins and a correlation of the amino acid sequences of rat and yeast ribosomal proteins.

The covalent structure of the rat 40 S ribosomal subunit protein S12 was determined from the sequence of amino acids in tryptic, chymotryptic, thermolytic, and cyanogen bromide peptides and inferred from the sequence of nucleotides in a recombinant cDNA. Rat ribosomal protein S12 contains 129 amino acids and has a molecular weight of 14,120. The amino acid sequences of a number of ribosomal proteins appear to be related to rat S12. These include spinach chloroplast L7, Escherichia coli S5, Nicotiana tabacum chloroplast S18, and Bacillus stearothermophilus S12, and perhaps others. In addition, there are two sequences, 26 and 18 amino acids in length, in rat S12 that may be related to segments of the same number of residues in ribosomal proteins from a number of species. These, and other results, reinforce the suggestion that ribosomal proteins form an extended family.

Amino Acid Sequence↗

PubMed1987

The primary structure of rat ribosomal protein L7. The presence near the amino terminus of L7 of five tandem repeats of a sequence of 12 amino acids.

The covalent structure of rat ribosomal protein L7 was determined in part from the sequence of nucleotides in a recombinant cDNA and in part from the sequence of amino acids in portions of the protein. The complementary analyses supplemented and confirmed each other. Ribosomal protein L7 contains 258 amino acids and has a molecular weight of 30,040. The protein has an unusual and striking structural feature near the NH2 terminus: five tandem repeats of a sequence of 12 residues. Rat L7 appears to be related to ribosomal protein L7 from the moderate halophile Vibrio costicola and perhaps to L30 from Bacillus stearothermophilus, to L7 from the moderate halophile NRCC 41227, and to L22 from Nicotinia tobaccum chloroplast. In addition, there is a sequence of 24 amino acids in rat protein L7 that may be related to segments of the same number of residues in Escherichia coli ribosomal proteins S10, S15, L9, and L22.

Amino Acid Sequence↗

PubMed1987

The primary structure of rat ribosomal protein L5. A comparison of the sequence of amino acids in the proteins that interact with 5 S rRNA.

The covalent structure of rat ribosomal protein L5, which associates with 5 S rRNA in the organelle, was deduced from the sequence of nucleotides in a recombinant cDNA (pL5-6-4) and confirmed from the sequences of amino acids in portions of the protein. Ribosomal protein L5, encoded by pL5-6-4, contains 296 amino acids and has a molecular weight of 34,298. However, a second recombinant cDNA, pL5-8-5, encodes a protein with an additional methionyl residue at position 236 and may be the product of a second active L5 gene. Rat L5 is homologous to yeast YL3 and to Halobacterium cutirubrum HL13, proteins that also bind to 5 S rRNA. No significant structural similarity, however, was found between rat L5 and other 5 S rRNA-binding proteins; not with a second H. cutirubrum protein HL19, nor the Escherichia coli ribosomal proteins, L5, L18, or L25, nor the Xenopus laevis transcription factor IIIA. H. cutirubrum HL19, however, has structural identity with E. coli L5 and seems to be related to yeast YL3 and, hence, may be an evolutionary link between the prokaryotic and eukaryotic 5 S rRNA-binding proteins. A group of ribosomal proteins not known to be associated with 5 S rRNA are also related to rat L5. They include: rat L39, Euglina gracilis chloroplast S7, Saccharomyces cerevisiae L31 and L46, Homo sapiens L32 and, perhaps, several others as well. There is an especially close interrelationship between rat L5, rat L39, yeast L46, human L32, and mouse L32. These results, and others, suggest that ribosomal proteins form an extended family and that L5 may contain in its structure traces of this affinity.

Amino Acid Sequence↗

PubMed1987

The primary structure of rat ribosomal protein L19. A determination from the sequence of nucleotides in a cDNA and from the sequence of amino acids in the protein.

The covalent structure of rat ribosomal protein L19 was inferred from the sequence of nucleotides in a recombinant cDNA and confirmed from the sequence of amino acids in a portion of the protein. Ribosomal protein L19 contains 196 amino acids and has a molecular weight of 26,971. There are indications that a segment of 23 residues in rat L19 is related to sequences of the same length in Escherichia coli ribosomal proteins L30, L18, and S2.

Amino Acid Sequence↗

PubMed1987

Relative bioavailability of rimantadine HCl tablet and syrup formulations in healthy subjects.

Twenty healthy male subjects completed an open-label randomized crossover design to assess the bioavailability of 100 mg of rimantadine HCl in tablet and syrup forms relative to an oral solution. Blood samples were drawn and rimantadine plasma concentrations were determined by a GC-MS method. The maximum plasma concentration (Cmax), the time to Cmax (tmax), the area under the plasma concentration-time curve (AUC), and k were compared among treatments using an analysis of variance and the Hauck-Anderson test for bioequivalence. The Hauck-Anderson test was satisfied when the syrup and solution were compared. The relative bioavailability of the syrup was 96%. Both Cmax and AUC were significantly (p less than 0.05) increased (23 and 17%, respectively) when the tablet was compared with the solution. The relative bioavailability of the tablet was 117%. This outcome was unusual and could not be explained. However, this was not anticipated to be of clinical consequence since the majority of the safety and efficacy of rimantadine HCl was established using a tablet.

Adamantane↗

PubMed1987

Pharmacokinetics of rimantadine hydrochloride in patients with chronic liver disease.

Six patients with chronic liver disease and six sex-, age (+/- 5 years)-, and weight (+/- 5 kg)-matched healthy control subjects received a single dose of two 100 mg tablets rimantadine HCl. Eight additional patients with chronic liver disease who were not matched to healthy subjects received a single dose of two 100 mg tablets of rimantadine HCl. Blood and urine samples were collected and rimantadine concentrations were determined by a GCMS method. The values for maximum plasma concentration, AUC, elimination half-life, and renal clearance were not significantly different between patients and control subjects, independent of the statistical analyses (parametric and nonparametric) used. The mean apparent elimination half-life, volume of distribution, and total clearance in the matched patients with liver disease were 32 hours, 24 L/kg, and 676 ml/min, respectively. Renal clearance and the amount excreted in the urine unchanged were 63 ml/min and 10%, respectively. In conclusion, rimantadine pharmacokinetics were not appreciably altered in patients with less severe chronic liver disease.

Adamantane↗

PubMed1986

Relative and absolute bioavailability of cibenzoline capsules and tablets in healthy subjects.

Eighteen healthy adult volunteers completed an open-label, four-way crossover study designed to determine the bioequivalency of 160-mg cibenzoline [2-(2,2-diphenylcyclopropyl)-4,5-dihydro-1H-imidazole] capsules and tablets, their relative bioavailability compared with an oral solution of the drug, as well as the absolute bioavailability of these dosage forms compared with an intravenous infusion of the drug. Blood samples obtained at specified times after drug administration were assayed for cibenzoline by HPLC, and pharmacokinetic parameters were estimated from the resulting plasma concentration-time profiles. Comparisons were made between the tablet and capsule to assess bioequivalency, between the solid dosage forms and a solution to assess relative bioavailability, and between the oral forms and an intravenous infusion to assess absolute bioavailability. The pharmacokinetic parameters for each oral dosage form were similar and ratios of mean parameters indicated that the solid dosage forms were bioequivalent and completely bioavailable relative to an oral solution. The ratios of the area under the plasma concentration-time profiles (AUC) for the capsule, tablet, and oral solution to that of the intravenous infusion were 0.85, 0.83, and 0.86, respectively, indicating that orally administered cibenzoline has an absolute bioavailability of approximately 85%.

Adult↗

PubMed1986

Effect of food on cibenzoline bioavailability.

Eighteen healthy adult volunteers received 160 mg oral capsule doses of cibenzoline in an open-label, four-way randomized crossover study designed to determine the influence of food on cibenzoline pharmacokinetics. Cibenzoline was administered 1 h prior to, with, and 1 h following a standard breakfast as well as under fasting conditions. There was no change in any bioavailability parameter when the data following drug ingestion 1 h prior to food were compared to the fasted state. Bioavailability parameters obtained when drug was taken during the meal or 1 h after the meal suggested that the rate of absorption was slightly decreased in the presence of food, while the extent of absorption was unaltered. The decreased absorption rate in the presence of food is not expected to be of clinical significance. The presence of food is not expected to affect the bioavailability of cibenzoline to the extent of clinical significance.

Adult↗

PubMed1986

Strategy and abilities training for prose recall and comprehension in mentally retarded children.

This study compared the effects of training conditions, abilities, strategies, and a combination of abilities and strategies on the recall and comprehension of prose passages. The subjects were 45 educable mentally retarded children divided equally into the three conditions. Although there was significant pre- to post-test improvement within each condition for factual recall, no differences were observed among the conditions for either factual recall or comprehension.

Child↗

PubMed1984

The primary structure of rat liver ribosomal protein L39.

The covalent structure of the rat liver 60 S ribosomal subunit protein L39 was determined. Fourteen tryptic peptides were purified, and the sequence of each was established by a micromanual procedure; they accounted for all 50 residues of L39. The sequence of the NH2-terminal 32 residues of L39, obtained by automated Edman degradation of the intact protein, provided the alignment of the first seven tryptic peptides. Two peptides, CNI (28 residues) and CNII (22 residues), were produced by cleavage of protein L39 with cyanogen bromide and the sequence of CNII was determined by automated Edman degradation. This sequence established the order of tryptic peptides T8 through T14. The carboxyl-terminal amino acids were identified after carboxypeptidase A treatment. Protein L39 contains 50 amino acids and has a molecular weight of 7308. There are indications that a portion of rat L39 is related to a fragment of Escherichia coli ribosomal protein S1.

Animals↗

PubMed1983

The primary structure of rat liver ribosomal protein L37. Homology with yeast and bacterial ribosomal proteins.

The covalent structure of the rat liver 60 S ribosomal subunit protein L37 was determined. Twenty-four tryptic peptides were purified and the sequence of each was established; they accounted for all 111 residues of L37. The sequence of the first 30 residues of L37, obtained previously by automated Edman degradation of the intact protein, provided the alignment of the first 9 tryptic peptides. Three peptides (CN1, CN2, and CN3) were produced by cleavage of protein L37 with cyanogen bromide. The sequence of CN1 (65 residues) was established from the sequence of secondary peptides resulting from cleavage with trypsin and chymotrypsin. The sequence of CN1 in turn served to order tryptic peptides 1 through 14. The sequence of CN2 (15 residues) was determined entirely by a micromanual procedure and allowed the alignment of tryptic peptides 14 through 18. The sequence of the NH2-terminal 28 amino acids of CN3 (31 residues) was determined; in addition the complete sequences of the secondary tryptic and chymotryptic peptides were done. The sequence of CN3 provided the order of tryptic peptides 18 through 24. Thus the sequence of the three cyanogen bromide peptides also accounted for the 111 residues of protein L37. The carboxyl-terminal amino acids were identified after carboxypeptidase A treatment. There is a disulfide bridge between half-cystinyl residues at positions 40 and 69. Rat liver ribosomal protein L37 is homologous with yeast YP55 and with Escherichia coli L34. Moreover, there is a segment of 17 residues in rat L37 that occurs, albeit with modifications, in yeast YP55 and in E. coli S4, L20, and L34.

Amino Acid Sequence↗

PubMed1983

Far generalization of visual analogies strategies by impulsive and reflective EMR students.

Cognitive style and its interaction with training effects in promoting the acquisition and far generalization of a visual analogies strategy by 22 male and 17 female EMR pupils was evaluated. Training was effective in producing acquisition and far generalization; cognitive style was not. We suggested that the lack of interaction between cognitive style and training was due to the fact that the training program modified the subjects' cognitive style, i.e., impulsives tended to perform more like reflectives.

Adolescent↗

PubMed1982

The primary structure of the acidic phosphoprotein P2 from rat liver 60 S ribosomal subunits. Comparison with ribosomal 'A' proteins from other species.

The primary structure of rat liver ribosomal protein P2 was deduced from the sequence of the peptides. Ten peptides were obtained by cleavage of P2 with trypsin. The peptides, which accounted for the 111 residues of P2, were isolated by high voltage electrophoresis and chromatography on cellulose thin layer sheets, and the partial or complete sequence was determined by micromanual or solid-phase procedures using 4-N,N-dimethylaminoazobenzene 4'-isothiocyanate and phenylisothiocyanate. In a similar manner, the sequence of 14 peptic peptides was determined. The sequence of the NH2-terminal 30 residues of P2 was obtained by automatic Edman degradation in a sequenator. The ordering of the tryptic peptides was aided by determination of the partial or complete sequence of fragments generated with chymotrypsin, or Armillaria mellea protease, or by secondary cleavage of peptic peptides with trypsin. The carboxyl-terminal sequence was obtained from a cyanogen bromide fragment and from hydrolysis with carboxypeptidase. The sequence of protein P3 was also determined. P3 differs from P2 only in that it lacks the carboxyl-terminal 8 residues, and hence, it is likely to be a proteolytic product of P2. Rat liver ribosomal protein P2 is homologous with yeast YP A1, with Artemia salina eL12, and with Halobacterium cutirubrum L20. It is likely that rat liver P2 is also homologous with the prokaryotic ribosomal "A" proteins, Escherichia coli L7/L12, Micrococcus lysodeikticus MA1, and Bacillus subtilis L9, but that during evolution, a transposition of a portion of the molecule occurred.

Amino Acid Sequence↗

PubMed1982

Symptomatic large parietal foramina.

A mother and her two children with large parietal foramina were studied with plain roentgenograms and computed tomography. The mother's comments convinced us that the bilateral defects in the children evolved from a single midline opening via median ossification. The children had recurrent bouts of unexplained headaches and vomiting. Gentle pressure over the defects and combining of the overlying hair produced local pain and violent headaches in all three patients. These characteristic symptoms as well as other clinical problems associated with this anomaly are discussed.

Adult↗

PubMed1980

Identification by affinity chromatography of the rat liver ribosomal proteins that bind to Escherichia coli 5 S ribosomal ribonucleic acid.

The eukaryotic and prokaryotic ribosomal proteins that bind to Escherichia coli 5 S rRNA were identified by affinity chromatography. The E. coli ribosomal proteins that associated with the nucleic acid were L5, L18, and L25 confirming earlier findings using the same and different procedures. The rat liver ribosomal proteins that associated with E. coli 5 S rRNA were L6, L7, L19, L35a, and S9; several of those proteins also bind to rat liver 5 S rRna (L6, L19) and to 5.8 S rRna (L6, L19, and S9).

Animals↗

PubMed1980

Facilitating a therapeutic milieu in the families of schizophrenia.

For many years, mental health professionals and the families of schizophrenics have coexisted in an atmosphere of mutual distrust and hostility. In this paper, we would like to present some of our experiences in creating a more productive relationship with the families of long-term schizophrenic clients in an aftercare setting. We have found that it is possible to engage these families as allies in the long and difficult process of psychodynamically oriented psychotherapy and resocialization. In many instances, these families actually provide several of the major functions of a vital therapeutic milieu, including containment, support, and structure (Gunderson, 1978).

Adult↗

PubMed1979

Identification by affinity chromatography of the eukaryotic ribosomal proteins that bind to 5.8 S ribosomal ribonucleic acid.

The proteins that bind to rat liver 5.8 S ribosomal ribonucleic acid were identified by affinity chromatography. The nucleic acid was oxidized with periodate and coupled by its 3'-terminus to Sepharose 4B through and adipic acid dihydrazide spacer. The ribosomal proteins that associate with the immobilized 5.8 S rRNA were identified by polyacrylamide gel electrophoresiss: they were L19, L8, and L6 from the 60 S subunit; and S13 and S9 from the small subparticle. Small amounts of L14, L17', L18, L27/L27', and L35', and of S11, S15, S23/S24, and S26 also were bound to the affinity column, but whether they associate directly and specifically with 5.8 S rRNA is not known. Escherichia coli ribosomal proteins did not bind to the rat liver 5.8 S rRNA affinity column.

Animals↗

PubMed1979

Isolation of eukaryotic ribosomal proteins: purification and characterization of S25 and L16.

Proteins were extracted from rat liver ribosomal subunits with ethanol and ammonium chloride. The extract from the 40S subunit contained mainly S25, but smaller amounts of a number of other proteins were found as well; the extract from the 60S subparticle had L16 in addition to P1, P2, S25, and several other proteins. S25 and L16 had not been purified before. The former was isolated from the ethanol-ammonium chloride extract by stepwise elution from carboxymethylcellulose with LiCl, chromatography on phosphocellulose, and filtration through Sephadex G-75; L16 was purified by elution from carboxymethylcellulose with LiCl (in steps). The molecular weight of the two proteins was estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate; and amino acid composition was determined also.

Amino Acids↗