PubMed Health⌕ Search

Biomedical subjects

A S Cook

Publications and source records attributed to A S Cook.

10 recordsLinked to original sources
PubMed1988

Variation in the biologic and biochemical characteristics of human menopausal gonadotropin.

Lot differences in the biopotency of human menopausal gonadotropin (hMG) were evaluated and the potential biochemical basis was investigated. The in vivo biopotency of hMG was assessed by a unique bioassay that evaluates the number of ova shed in the cyclic hamster in response to hMG administration. Significant variation in hMG lots was observed using this assay. When subjected to chromatofocusing, hMG displayed five immunoreactive follicle-stimulating hormone (FSH) isohormones and nine luteinizing hormone (LH) isohormones. The relative distribution of FSH, but not LH isohormones, was slightly but significantly different between the lots tested. These data indicate that significant differences exist in the ability of commercially available hMG to stimulate follicular development and ovulation. The biochemical basis for these differences in in vivo biopotency remains to be elucidated.

Animals↗
PubMed1982

Implications of ethnicity in the care of the terminally ill.

A holistic approach to the care of the terminally ill must include considerations of ethnic variables and cultural traditions influencing views of death. The implications of ethnicity for health care delivery, direct patient care, and interpretation of patient and family responses are discussed.

Attitude to Death↗
PubMedDate not supplied

Analysis of chromatin proteins from human placenta.

Low-salt extracts of chromatin from human term placenta have been examined for the presence of the high mobility group (HMG) proteins. Based upon salt-dissociation characteristics, solubilities in trichloroacetic acid and electrophoretic behaviour on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and non-equilibrium pH gradient gel electrophoresis (NEPHGE), each of the HMG proteins is present, including HMG-1, -2, -E, -14, and -17. A remarkably large amount of HMG-E is present in term human placenta. Additionally, a protein not previously recognized, which we designate HMG-PL, is present in term placenta. Electrophoretic comparison of the HMG proteins from placentae of varying gestational age, using NEPHGE, demonstrates that all of the placental HMG proteins exhibit multiplicity, reminiscent of chicken erythrocyte HMG proteins. Specifically, we found HMG-E to be unaltered in amounts relative to HMG-1 and -2 in placentae varying from 20 to 40 weeks of gestation. HMG-PL, however, is differentially expressed, increasing in amounts as gestation proceeds past 34 weeks. HMG-PL was purified and subjected to amino acid analysis. Its composition supports the notion that HMG-PL is a member of the HMG-1 family.

Amino Acids↗