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Biomedical subjects

M Richardson

Publications and source records attributed to M Richardson.

At least 271 records · Page 15Linked to original sources
PubMed1992

The amino acid sequences of two 13-kDa alpha-amylase inhibitors from the seeds of Sorghum bicolor (L.) Moench.

Two inhibitors (SI alpha 4 and SI alpha 5) of the alpha-amylases from insect and mammalian sources were purified from seeds of Sorghum bicolor by saline extraction, precipitation with ammonium sulphate, affinity chromatography on Red Sepharose, and preparative and analytical reverse-phase HPLC on columns of Vydac C18. The complete primary structures of these two inhibitors were determined by automated degradation of the intact, reduced and S-alkylated proteins and by manual 4-N,N-dimethylaminoazobenzene-4-isothiocyanate/phenyl isothiocyanate microsequencing of peptides derived from them following enzyme digests. The amino acid sequences were as follows: SI alpha 4: TVDVTACAPGLAIPAPPLPTCRTFARPRTCGLGGPYGPVDPSPVLKQ- RCCRELAAVPSRCRCAALGFMMDGVDAPLQDFRGCTREMQRIYAVSRLTRAAECNLPTIPGGGCHLSNS PR; and SI alpha 5: ANWCEPGLVIPLNPLPSCRTYMVRRACGVSIGPVVPLPVLKERCCSELEKLV- PYCRCGALRTALDSMMTGYEMRPTCSWGGLLTFAPTIVCYRECNLRTLHGRPFCYALGAEGTTT. Comparisons of these sequences with one another and with those of other proteins in the US National Biomedical Research Foundation Databank indicated that the two Sorghum proteins had significant similarities (21%-42% identity) with the members of the cereal superfamily of enzyme inhibitors.

Amino Acid Sequence↗
PubMed1992

Identification of developmental disabilities and health problems among individuals under child protective services.

Although a relation between child abuse and developmental disabilities has been established, information about the health and developmental status of children referred to child protective services is not adequately obtained. Case records of 150 children identified to child protective services were reviewed in order to determine the availability of health and developmental information. A screening protocol was developed for the purpose of reviewing case records that has potential for use by child protective services workers.

Adolescent↗
PubMed1992

Altered levels of antithrombin III and fibrinogen in the aortic wall of the alloxan-induced diabetic rabbit: evidence of a prothrombotic state.

The distribution and behavior of the rabbit plasma proteins albumin, fibrinogen, and antithrombin III (ATIII) (isoforms alpha and beta), have been examined in groups of alloxan-induced diabetic rabbits and control rabbits. By injecting radiolabeled preparations intravenously, measurements of plasma clearance, rates of catabolism, and compartmental distribution were made for each protein. In addition, after allowing the radiolabeled proteins to circulate for 12 hours, we excised aortas after exsanguination and determined the content of these proteins in the endothelium and subendothelium. The respective fractional catabolic rates of ATIII-alpha and ATIII-beta were similar in the diabetic and control rabbits, but fibrinogen and albumin were catabolized more slowly in the diabetic rabbit than in the control rabbit. The distributions of albumin and the ATIII isoforms between the intravascular, noncirculating vascular, and extravascular compartments in the diabetic rabbit were similar to the respective proteins in the control rabbit, but a smaller proportion of fibrinogen was associated with the vascular compartment of the diabetic rabbit when compared with that in the control rabbit. At 12 hours after injection, the quantities of fibrinogen and albumin associated with the diabetic aorta endothelium and particularly the subendothelium were increased, whereas ATIII-alpha and ATIII-beta were decreased relative to the control aorta. The fibrinogen-to-ATIII ratio in the diabetic aorta was increased twofold to threefold when compared with that in the control aorta. We conclude that the increased ratio of fibrinogen to ATIII in the aorta wall of the diabetic rabbit may be characteristic of the prothrombotic state that is conspicuous in insulin-dependent diabetes.

Albumins↗