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Biomedical subjects

A G Lloyd

Publications and source records attributed to A G Lloyd.

36 records · Page 2Linked to original sources
PubMed1972

The metabolism of sodium cortisone 21-( 35 S)sulphate in the rat.

1. The metabolism of sodium cortisone 21-[(35)S]sulphate was investigated in rats. 2. Quantitative and qualitative experiments showed that substantial amounts of (35)SO(4) (2-) appeared in the urine of free-ranging rats receiving the ester. 3. Whole-body radioautograms indicated considerable biliary elimination of (35)S and also pointed to the liver as the site of metabolism. 4. When female rats with bile-duct cannulae received sodium cortisone 21-[(35)S]sulphate approx. 70% of the dose appeared in the bile as a doubly conjugated steroid (metabolite I). This metabolite was identified as 3alpha-(beta-d-glucopyranuronosido)- 17alpha-hydroxy-21-[(35)S]sulpho-oxy-5alpha-pregnane-11,20-dione. 5. When metabolite I was administered to a rat with a bile-duct cannula 90% of the dose appeared in the bile unchanged. After the administration (intraperitoneally or orally) of metabolite I to free-ranging rats considerable amounts of (35)SO(4) (2-) appeared in the urine. 6. The route by which (35)SO(4) (2-) might be produced from cortisone [(35)S]sulphate in free-ranging animals is discussed.

Animals↗
PubMed1968

The glycosulphatase of Trichoderma viride.

The growth of the mould Trichoderma viride on a defined medium containing either potassium d-glucose 6-O-sulphate or potassium d-galactose 6-O-sulphate as sole sources of both carbon and sulphur is marked by the production of an enzyme system capable of liberating inorganic SO(4) (2-) ions from either of the sulphate esters. The enzyme is not produced when the organism is grown with glucose (or galactose) and potassium sulphate or with glucose and methionine as sole sources of carbon and sulphur. Experimental conditions are described whereby inorganic SO(4) (2-) ions liberated from potassium glucose 6-O-sulphate by the growing mould appear in the culture medium after a constant lag period of 21-24hr. The enzyme has been shown to be a simple glycosulphatase that is active towards the 6-O-sulphate esters of d-glucose and d-galactose but not towards potassium glucose 3-O-sulphate. The properties of the crude glycosulphatase show the enzyme to be appreciably different from analogous molluscan enzymes that can degrade monosaccharide sulphate esters.

Carbohydrates↗