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Biomedical subjects

G Allen

Publications and source records attributed to G Allen.

At least 145 records · Page 8Linked to original sources

Analysis and purification of human lymphoblastoid (Namalwa) interferon using a monoclonal antibody.

Highly purified interferon-alpha (IFN-alpha) prepared from a human lymphoblastoid line (Namalwa) was analysed by gel filtration and polyacrylamide gel electrophoresis (PAGE). Gel filtration separated the IFN-alpha into two peaks (A and B). All the components of peak A were retained by a monoclonal antibody (NK2) column, but some of those from peak B were not retained. The IFN that was not bound was active on mouse cells and could be resolved into two major bands by PAGE. The bound fraction (about 75% of the interferon protein) was purified by means of the monoclonal antibody column, although complete purification of crude interferon was not achieved in one passage.

Antibodies, Monoclonal↗

Macrophage production of prostaglandins: effects of fetal calf serum and diazepam. Use of an improved method for extracting 6-keto-PGF1 alpha.

Mouse peritoneal macrophages were incubated with varying amounts of heat-inactivated fetal calf serum (FCS) and treated with diazepam at the concentrations of 0.5 and 5.0 mug/ml. These macrophage preparations demonstrate that the capacity for synthesis and release of prostaglandins (PGs) E2, F2 alpha, 6-keto-PGF1 alpha and thromboxane TX(B2) is: (a) sensitive to the concentration of FCS in the culture medium, and (b) altered in the presence of diazepam. A radioimmunoassay for 6-keto-PGF1 alpha is also reported. The efficiency of extraction of PGE2 and 6-keto-PGF1 alpha from buffer or plasma samples was greatly improved when a petroleum ether/ether (1/1) solvent system was employed.

6-Ketoprostaglandin F1 alpha↗

Anxiety and mitral valve prolapse syndrome.

The diagnosis of Mitral Valve Prolapse Syndrome (MVPS), even though symptomatically similar to anxiety neurosis, may prompt pharmacological treatment only, neglecting any underlying emotional problems. If only a dichotomy were considered, one diagnosis might be seen as mutually exclusive of the other. A case history is presented illustrating features of both clinical syndromes. We consider the interaction of both etiologies, as well as the possibility of both being unrelated and coincidental. As physiological factors are explored when the diagnosis of anxiety neurosis is considered, so should psychological factors be examined with MVPS.

Adult↗

Ruptured abdominal aortic aneurysm: an 11 year review.

This paper reviews experience over 11 years at Waikato Hospital of an aggressive approach to ruptured abdominal aortic aneurysms. The total hospital mortality was 51 percent. Of those reaching operation 34 percent died in hospital. This was reduced to 28 percent over the last five years of the survey. Features relating to the presentation, operative and postoperative management, and subsequent progress of patients are discussed.

Acute Kidney Injury↗

Specific activity of pure human interferons and a non-biological method for estimating the purity of highly purified interferon preparations.

Methods for determining the specific activity and percentage purity of highly purified interferon preparations are unreliable, mainly because of the difficulty in estimating very small quantities of protein. Human leukocyte-derived interferon (HuIFN-alpha) is a mixture of several distinct species, and the relationship between specific activity and purity is not direct. A non-biological method is described here, by which the purity of highly purified HuIFN-alpha is determined chromatographically. Samples are run on a Sephadex G-75 column with continuous measurement of E206 in the eluate, and SDS gel electrophoresis is used to separate essentially all the protein species in the characteristic double peak region containing interferon activity and show that they are interferons. The validity of the method has been checked using a range of standard proteins. The specific activity of pure Namalwa (lymphoblastoid) HuIFN-alpha was estimated to be 1.0--1.7 x 10(8) U/mg protein.

Cells, Cultured↗

Utilization of medical services after short-term psychiatric therapy in a prepaid health plan setting.

Utilization of medical services in Group Health Association of Washington, D.C., was analyzed for patients referred in 1970 for short-term psychiatric therapy under benefits but who had no therapy or referral for at least the 12 preceding months. A matched comparison group and family members were also studied. Medical visits were analyzed in three time periods: the 12 months preceding referral, the next 4 months when therapy was likely to be received, and a final 12 months. Compared with controls, the Index Cases did not show a significant reduction of "offset" in utilization of outpatient medical services after referral, but they did decreases days of medical hospitalization significantly. When Index Cases were divided into low and high users of psychiatric therapy, the former showed a decline, the latter an increase in medical visits, and the difference between them was significant. The before-after change in utilization among other family members was similar to that for index and control subjects. The findings suggest the need to identify the types of patient and the clinical settings which are most likely to maximize the offset effect of brief psychotherapy. Medical care programs should be tailored to meet the different psychotherapy. Medical care programs should be tailored to meet the different psychiatric needs of these and other patients in an effective and efficient manner.

Adolescent↗

A family of structural genes for human lymphoblastoid (leukocyte-type) interferon.

Amino acid sequences of tryptic and chymotryptic peptides from human lymphoblastoid interferon (IFN-alpha) have been determined. The results show that IFN-alpha consists of a family of proteins with at least five different, but homologous, primary structures. There appears to be little, if any, glycosylation of the major components of IFN-alpha.

Amino Acid Sequence↗

The primary structure of the calcium-transporting adenosine triphosphatase of rabbit skeletal sarcoplasmic reticulum. Soluble tryptic peptides from the succinylated carboxymethylated protein.

The isolation and the determination of the amino-acid sequences of the soluble tryptic peptides, derived by cleavage at arginine residues, of the succinylated (3-carboxypropionylated) S-carboxymethylated adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum are described. Treatment of the protein with succinic anhydride gave a derivative that was readily digested with trypsin, yielding two distinct sets of peptides. One set comprises large, relatively hydrophobic, peptides that are highly aggregated (or insoluble) in aqueous solution and that have been identified, by several criteria, with the portion of the protein embedded in the lipid bilayer in the sarcoplasmic reticulum. The second set, which is described here, comprises peptides that have properties typical of those derived from soluble globular proteins and that constitute that part of the protein external to the lipid bilayer. The sequences of these soluble tryptic peptides contain 586 unique residues. Details of the isolation of the peptides and the determination of the sequences are contained in Supplementary Publication SUP 50102 (88 pages) which has been deposited with 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↗

Primary structure of the calcium ion-transporting adenosine triphosphatase of rabbit skeletal sarcoplasmic reticulum. Soluble peptides from the alpha-chymotryptic digest of the carboxymethylated protein.

The isolation of the soluble peptides from the chymotryptic digest of the calcium-transporting ATPase of rabbit skeletal sarcoplasmic reticulum is described. These peptides were partially sequenced and the information obtained was used to align tryptic peptides of the protein and to confirm sequences within the tryptic peptides. Details of the isolation of some peptides and the amino acid analyses of the peptides are given in Supplementary Publication SUP 50103 (10 pages), which has been deposited with 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↗

Primary structure of the calcium ion-transporting adenosine triphosphatase from rabbit skeletal sarcoplasmic reticulum. Some peptic, thermolytic, tryptic and staphylococcal-proteinase peptides.

The soluble peptides from the peptic digest of the reduced S-carboxymethylated 3-carboxypropionylated adenosine triphosphatase protein have been isolated and most of their structures have been determined. About 397 residues of the protein were represented in these peptides. The reduced S-carboxymethylated protein was digested with thermolysin, and peptides containing arginine or carboxymethylcysteine were isolated and characterized. Some peptides isolated from tryptic and staphylococcal-proteinase digests of the protein are described. The information contained within the structures of these peptides has been used to reconstruct long stretches of the sequence of the ATPase protein that constitute most of the protein structure external to the lipid bilayer (Allen, Trinnaman and Green (1980) Biochem. J. 187, 591-616). The details of some of the chromatographic steps used in the isolation of the peptides and the properties of the peptides are contained in Supplementary Publication SUP 50104 (45 pages), which has been deposited with 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↗

The primary structure of the calcium ion-transporting adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum. Peptides derived from digestion with cyanogen bromide, and the sequences of three long extramembranous segments.

The isolation and characterization of the soluble peptides from the CNBr digest of the calcium ion-transporting adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum are described. The 562 unique residues of the protein were placed in sequences. The remaining part of the protein (about 500 residues) yielded long hydrophobic sequences that contained all but one of the tryptophan residues of the protein and that were probably derived largely from the intramembranous parts of the protein. Three long stretches of primary structure, constituting half of the protein, have been reconstructed from the information presented here together with the sequences found in peptides from other digests of the protein. The secondary structures of these sequences have been predicted. A model for the primary structure of the protein is presented and the implications discussed. Details of the isolation of peptides are contained in Supplementary Publication, SUP 50105 (29 pages), which has been deposited with 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↗