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Biomedical subjects

G Francis

Publications and source records attributed to G Francis.

At least 109 records · Page 6Linked to original sources
PubMed1979

Effects of gas density on the frequency response of gas-filled pressure transducers.

The effects of gas density on the frequency responses of four pressure transducers were determined at gas densities from 1.2 to 25.0 g/l. Transducers tested included three sensitive differential types used with pneumotachographs to measure respiratory flow (Validyne DP-45 and DP-103; Medistor P-11) and a transducer commonly used to measure esophageal pressure (Statham P23Dd). Three different responses were obtained. The Validyne DP-103 was overdamped and its response was essentially independent of gas density. The frequency response of this transducer is adequate for use with quiet breathing only. The Validyne DP-45 and Medistor P-11 responses were underdamped. The resonant peaks of these transducers decreased markedly in frequency as the gas density increased. The Statham P23Dd was also underdamped; however, its resonant frequency increased as gas density increased. An esophageal balloon did not alter the frequency response characteristics of this tubing-transducer system. Both increases in length and decreases in diameter of connecting tubing reduced the frequency of resonant peaks of underdamped pressure transducers.

Atmospheric Pressure↗
PubMed1978

The covalent structure of cartilage collagen. Amino acid sequence of residues 552-661 of bovine alpha1(II) chains.

The covalent structure of the first 111 residues from the N-terminus of peptide alpha1(II)-CB10 from bovine nasal-cartilage collagen is presented. This region comprises residues 552-661 of the alpha1(II) chain. The sequence was determined by automated Edman degradation of peptide alpha1(II)-CB10 and of peptides produced by cleavage with trypsin and hydroxylamine. Comparison of this region of the alpha1(II) chain with the homologous segment of the alpha1(I) chain indicated a homology level of 85%, slightly higher than that of 81% reported for the N-terminal region of the alpha1(II) chain (Butler, Miller & Finch (1976) Biochemistry15, 3000-3006). The occurrence of two residues of glycosylated hydroxylysine was established at positions 564 and 603, the first present exclusively as galactosylhydroxylysine and the latter as a mixture of galactosylhydroxylysine and glucosylgalactosylhydroxylysine. Also, two residues at positions 648 and 657 were tentatively identified as glycosylated hydroxylysines. The amino acid sequences adjacent to the hydroxylysine residues so far identified in the alpha1(II) chain were compared with the homologous regions of the alpha1(I) and alpha2 chains, but no obvious prerequisite for hydroxylation could be seen. From comparison with the homologous sequence of the alpha1(I) chain, it appears that the alpha1(II)-chain sequence presented here contains three more amino acids than that reported for the alpha1(I) chain. This triplet would be interposed between residues 63 and 64 of the reported sequence of peptide alpha1(I)-CB7 from calf skin collagen. Data on the purification of the subpeptides and their amino acid compositions have been deposited as Supplementary Publication SUP 50087 (7 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

Amino Acid Sequence↗
PubMed1976

Abnormally soluble collagen produced in fibroblasts cultures.

Abnormally soluble collagen is synthesized in vitro not only by skin fibroblasts of Marfan patients but also by those of patients with Ehlers-Danlos type V and cutis laxa. The excessive solubility of collagen is corrected by the addition to the culture medium of a synthetic flavonoid, (+)- catechin.

Benzopyrans↗
PubMed1975

Isolation and chemical characterization of collagen in bovine pulmonary tissues.

1. The contents of the fibrous proteins collagen and elastin in the pleural and parenchymal regions of bovine lungs were determined. The collagen content was approx. 70% (g/100g of salt-extracted defatted powder) in each tissue, and the elastin content was 28% in pleura and 13.5% in parenchyma. 2. Purification of the insoluble collagen from the pleura and parenchyma of bovine lungs by various methods was attempted. The collagen fractions isolated after incubation of the pulmonary tissues with the proteolytic enzymes collagenase ("collagenase-soluble" fraction) or pancreatic elastase ("elastase-insoluble" fraction) each contained approx. 87% of the total collagen initially present. 3. Both collagen fractions were chemically analysed for their amino acid and carbohydrate contents and were found to be similar to those of the intact interstitial collagens isolated from skin, bone and tendon. 4. The contents of the two aldimine cross-linking compounds, dehydrohydroxylysinonorleucine and dehydrodihydroxylysinonorleucine, were determined in the bovine pulmonary collagen fractions, and were found to decrease with increasing age of the animals, and were similar to the values found in intact collagens from bone and tendon.

Amino Acids↗
PubMed1975

Isolation and characterization of acidic structural glycoproteins in pulmonary tissues.

1. Extraction of the pleural and parenchymal regions of bovine lungs with salt and organic solvents gave powders that contained glycoproteins in addition to collagen and elastin. The contents of these glycoproteins (g/100 of powder) was 4% in pleura and 15.5% in parenchyma. 2. Attempts were made to purify these glycoproteins fromboth tissues by various methods. 3. Both tissues contained heterogeneous mixtures that were similar solubilities, had similar amino acid and carbohydrate compostions. 4. The compostions of the pulmonary glycoproteins resembled those isolated from other connective tissues by other workers.

Amino Acids↗
PubMed1975

Lysyl oxidase deficiency in Ehlers-Danlos syndrome type V.

Two maternal cousins affected by the X-linked form of Ehlers-Danlos syndrome have been observed. Both had congenital heart disease, "floppy valve syndrome", hernias, short stature, stretchable skin and moderate joint hypermobility. Both excreted normal amounts of urinary glycosaminoglycans, almost entirely represented by dermatan sulfate, whose degradation appeared to be inadequate. They also excreted large amounts of hydroxylysine glycosides and L-valyl-proline, considered to be products of degradation of collagen and elastin, respectively. Cultured skin fibroblasts of the propositus synthesized excessively soluble collagen and had a low lysyl oxidase activity. These findings suggest that the increased degradation of structural proteins may be secondary to the defective cross-linking processes caused by the enzymic defect. Addition of (+) catechin, a flavonoid, to the propositus's cultured fibroblasts decreased the abnormal solubility of their collagen.

Amino Acid Oxidoreductases↗