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Biomedical subjects

A Lin

Publications and source records attributed to A Lin.

At least 37 records · Page 2Linked to original sources
PubMed1989

The primary structure of rat ribosomal protein S10.

The amino acid sequence of rat ribosomal protein S10 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. Ribosomal protein S10 contains 165 amino acids and has a molecular mass of 18917 Da. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 17-20 copies of the S10 gene. The mRNA for the protein is about 750 nucleotides in length. Ribosomal protein S10 has several possible internal duplications; one is a tandem repeat of ten residues that is basic and contains two or three prolines.

Amino Acid Sequence↗
PubMed1989

The pharmacokinetics and dose proportionality of cilazapril.

1. The pharmacokinetics and dose proportionality of cilazapril, an orally active angiotensin-converting enzyme (ACE) inhibitor, were investigated in a four-way randomized crossover study in 24 volunteers, over the 0.5 to 5 mg dose range intended for therapeutic use. 2. Plasma concentrations of cilazapril and of the active metabolite cilazaprilat together with plasma ACE activity were determined by radio-enzymatic assay. 3. Plasma concentrations of both cilazapril and cilazaprilat increased in proportion to dose over the range studied. All doses produced substantial inhibition of ACE. Higher doses were associated with earlier onset and longer duration of maximal effect.

Administration, Oral↗
PubMed1989

The influence of food on the pharmacokinetics and ACE inhibition of cilazapril.

1. The influence of food on the pharmacokinetics and angiotensin-converting enzyme (ACE) inhibitory effects of oral 5 mg doses of cilazapril was investigated in a two-way crossover study in 16 volunteers. 2. Plasma and urine concentrations of cilazaprilat, the active diacid metabolite of cilazapril, and plasma ACE activity were determined by a radio-enzymatic method. 3. Cmax decreased by 30% (P less than 0.05) with a delay in (t)max of 1 h (P less than 0.05) and area under curve (AUC) was decreased by 14% (P less than 0.05). The elimination rate was unaltered. 4. Onset of ACE inhibition was delayed by approximately 30 min but degree and duration were unaffected. 5. The effect of food on the bioavailability of cilazapril at this dose would not be expected to be clinically significant.

Adolescent↗
PubMed1988

The cytotoxins alpha-sarcin and ricin retain their specificity when tested on a synthetic oligoribonucleotide (35-mer) that mimics a region of 28 S ribosomal ribonucleic acid.

An oligoribonucleotide (35-mer) that mimics the alpha-sarcin and the ricin region of eukaryotic 28 S rRNA was transcribed in vitro from a synthetic template with T7 RNA polymerase and was used to test whether the specificity of the hydrolysis by the toxins was retained. alpha-Sarcin, at a low concentration, cleaved a single phosphodiester bond on the 3' side of a guanosine residue in the synthetic oligomer that corresponds to G-4325 in 28 S rRNA, the site of action of the toxin in intact ribosomes. At a high concentration of alpha-sarcin, the substrate (35-mer) was hydrolyzed after each of its purines. alpha-Sarcin was without an effect on a synthetic RNA (20-mer) that reproduces the near universal sequence of nucleotides in the loop, but lacks the stem, of the toxin's domain. Thus, the specificity of the attack of alpha-sarcin on a precise region of 28 S rRNA appears to be contingent on the sequence of the nucleotides and the structure of the domain. Ricin depurinated a nucleotide in the synthetic oligomer (35-mer), and in the presence of aniline the phosphoribose backbone was cleaved at a position that conforms to A-4324 in 28 S rRNA, the site of action of the toxin in vivo.

Base Sequence↗
PubMed1988

Primary structure of rat ribosomal protein L36a.

The amino acid sequence of rat ribosomal protein L36a, which may form part of the peptidyl transferase center, was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the amino-terminal amino acid sequence of the protein. Ribosomal protein L36a contains 105 amino acids (the amino-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 12,311. Hybridization of the cDNA to digests of nuclear DNA suggests that there are multiple copies of the L36a gene. Rat ribosomal protein L36a is homologous to a protein HL44 present in ribosomes of humans and protein 44 from Saccharomyces cerevisiae ribosomes.

Amino Acid Sequence↗
PubMed1988

Genetic disorders and major extracardiac anomalies associated with the hypoplastic left heart syndrome.

All pediatric autopsies of patients with hypoplastic left heart syndrome seen during an 11-year interval were reviewed to determine the frequency of underlying chromosomal and single-gene defects and idiopathic major extracardiac anomalies associated with this common, lethal congenital heart abnormality. Of 83 patients identified, nine had underlying chromosomal abnormalities, four had single-gene defects, ten had one or more major extracardiac anomalies without an identifiable chromosomal or mendelian disorder, and two were infants of insulin-dependent diabetic mothers. Overall, 23 patients (28%) had a genetic disorder and/or major extracardiac anomaly. The substantial prevalence of genetic causes of and major extracardiac anomalies associated with hypoplastic left heart syndrome underscores the need for a detailed genetic evaluation for all patients with hypoplastic left heart syndrome.

Abnormalities, Multiple↗
PubMed1987

The primary structure of rat ribosomal protein S8.

The amino acid sequence of rat ribosomal protein S8 was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2- and carboxyl-terminal amino acid sequences of the protein. Ribosomal protein S8 contains 207 amino acids (the NH2-terminal methionine is removed after translation of the mRNA) and has a molecular weight of 23,928. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 7-9 copies of the S8 gene. Ribosomal protein S8 contains a possible internal repeat that has 12 or 13 residues, is basic, and occurs 5 times in the protein.

Amino Acid Sequence↗
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↗