Biomedical subjects
S Hopkins
Publications and source records attributed to S Hopkins.
Clinical. A new approach to combat viruses.
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Antifungal agent for prostatic carcinoma.
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Serine hydroxymethyltransferase from Escherichia coli: purification and properties.
Serine hydroxymethyltransferase from Escherichia coli was purified to homogeneity. The enzyme was a homodimer of identical subunits with a molecular weight of 95,000. The amino acid sequence of the amino and carboxy-terminal ends and the amino acid composition of cysteine-containing tryptic peptides were in agreement with the primary structure proposed for this enzyme from the structure of the glyA gene (M. Plamann, L. Stauffer, M. Urbanowski, and G. Stauffer, Nucleic Acids Res. 11:2065-2074, 1983). The enzyme contained no disulfide bonds but had one sulfhydryl group on the surface of the protein. Several sulfhydryl reagents reacted with this exposed group and inactivated the enzyme. Spectra of the enzyme in the presence of substrates and substrate analogs showed that the enzyme formed the same complexes and in similar relative concentrations as previously observed with the cytosolic and mitochondrial rabbit liver isoenzymes. Kinetic studies with substrates showed that the affinity and synergistic binding of the amino acid and folate substrates were similar to those obtained with the rabbit liver isoenzymes. The enzyme catalyzed the cleavage of threonine, allothreonine, and 3-phenylserine to glycine and the corresponding aldehyde in the absence of tetrahydrofolate. The enzyme was also inactivated by D-alanine caused by the transamination of the active site pyridoxal phosphate to pyridoxamine phosphate. This substrate specificity was also observed with the rabbit liver isoenzymes. We conclude that the reaction mechanism and the active site structure of E. coli serine hydroxymethyltransferase are very similar to the mechanism and structure of the rabbit liver isoenzymes.
5,10-Methenyltetrahydrofolate synthetase. Purification and properties of the enzyme from rabbit liver.
The enzyme 5,10-methenyltetrahydrofolate synthetase has been purified to homogeneity from rabbit liver. The substrates are MgATP and 5-formyltetrahydrofolate. The enzyme will accept as substrates a variety of divalent metal ions and trinucleotides. The products of the reaction are 5,10-methenyltetrahydrofolate, ADP, and inorganic phosphate. The enzyme is a monomeric protein with a molecular weight of about 28,000. The stability of the enzyme is unusually sensitive to pH and ionic strength. Initial velocity studies suggest that the enzyme catalyzes a sequential mechanism. The turnover number of the enzyme is 300/min at 30 degrees C. The Km values for MgATP and 5-formyltetrahydrofolate are 0.3 mM and 0.5 microM, respectively. Product and dead-end inhibition studies indicate that substrates bind to the enzyme by a random mechanism. Vmax and the Km for MgATP are essentially constant over the pH range of 5.0-7.5. The results suggest that the enzyme catalyzes a reaction which serves as a salvage pathway to generate metabolically active one-carbon units from 5-formyltetrahydrofolate.
An antiemetic drug with a difference.
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Complications of the Ehlers-Danlos syndrome in pregnancy. A case report.
The Ehlers-Danlos syndrome (EDS) is a disorder of the connective tissue characterized by hyperextensible skin, loose jointedness, fragile tissues, bruising and bleeding diathesis. At least eight subtypes of EDS are recognized, each one with different clinical manifestations. On rare occasions EDS is associated with pregnancy. These patients are at risk for bleeding disorders and vascular, surgical and anesthetic complications as well as for premature labor, postpartum hemorrhage, bladder and uterine prolapse, abdominal hernias and wound dehiscence. We treated a pregnant patient for type 1 EDS and pregnancy-induced hypertension.
Pharmacology: pirenzepine.
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Transiderm-nitro.
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Localisation of collagen types and fibronectin in cartilage by immunofluorescence.
Collagens type I, II, III, IV, and V and the minor cartilage collagens, 1 alpha 2 alpha 3 alpha, C-PS 1, and C-PS 2, were purified, antibodies raised, and then used in immunofluorescence studies on bovine nasal cartilage (BNC). Punctate localisation was seen with the type II antibody. However, pretreatment of sections with hyaluronidase to remove the proteoglycan resulted in diffuse staining over all the section with this antibody. Antibodies to 1 alpha 2 alpha 3 alpha, C-PS 1, and C-PS 2 collagens gave no staining on untreated BNC sections, but after treatment with hyaluronidase all 3 antibodies showed as a diffuse 'halo' round each chondrocyte lacuna. Anti-type I, anti-type III, and anti-type IV collagen antibodies did not stain untreated or enzyme treated BNC. Type V collagen antibodies gave a bright ring in the pericellular region of the lacunae of hyaluronidase-treated BNC. This was unexpected, as we could not detect type V collagen biochemically in the same cartilage. Anti-fibronectin antibodies stained areas distant from the chondrocytes, these areas being distinct from those stained by 1 alpha 2 alpha 3 alpha and C-PS antibodies, suggesting that fibronectin is not associated with these collagens in BNC. These results suggest that different collagen types may have different locations within the cartilage matrix, that proteoglycans may inhibit antibody association with collagen, and that fibronectin is normally not associated with all types of collagen.
Bromocriptine and endocrine imbalance.
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Pharmacology: dantrolene sodium.
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