Maté tea inhibits in vitro pancreatic lipase activity and has hypolipidemic effect on high-fat diet-induced obese mice.

The inhibitory effects of maté tea (MT), a beverage produced with leaves from Ilex paraguariensis, in vitro lipase activity and on obesity in obese mice models were examined. For the in vitro experiment, porcine and human pancreatic lipase (PL) activities were determined by measuring the rate of release of oleic acid from hydrolysis of olive oil emulsified with taurocholate, phospholipids, gum arabic, or polyvinyl alcohol. For the in vivo experiments, animals were fed with a standard diet (SD, n = 10) or high-fat diet (HFD, n = 30) for 16 weeks.

Purification of bovine beta 2-microglobulin from colostrum and its complete amino acid sequence.

Bovine beta 2-microglobulin (beta 2-m) was purified from colostrum milk in two chromatographic steps: anion-exchange chromatography, and gel filtration. The amino acid sequence was determined to confirm that the purified protein was beta 2-m. A molecular weight of 11.

Somatolactin, a novel pituitary protein: isolation and characterization from Sparus aurata.

The complete amino acid sequence of somatolactin, a new pituitary protein belonging to the growth hormone/prolactin family, from the gilthead sea bream Sparus aurata has been determined. Somatolactin was isolated from the pituitary by alkaline extraction, gel filtration on a Sephadex G-100 column, and reversed-phase high-performance liquid chromatography (rpHPLC) on a TSK gel ODS-120T column. The purified protein was confirmed to be somatolactin by immunoblotting using chum salmon somatolactin antisera.

Complete amino acid sequence of crocodile growth hormone.

This paper describes the isolation and complete amino acid sequence of growth hormone (GH) from the pituitary gland of the crocodile, Crocodylus novaeguineae. GH was detected in an alkaline extract of the pituitary by specific immunoblot reactivity with rabbit antisera against cattle and salmon GH and isolated in pure form by DEAE-cellulose chromatography and by reversed-phase high-performance liquid chromatography. The yield of the GH was 2.

The complete amino acid sequence of pituitary cystatin from chum salmon.

Cystatin, a cysteine proteinase inhibitor, was isolated from chum salmon (Oncorhynchus keta) pituitary glands by ion-exchange chromatography on Mono-Q, gel filtration on Superdex 75, and reverse-phase HPLC on an ODS following ethanol-ammonium acetate extraction. Salmon pituitary cystatin was equipotent to chicken egg-white cystatin in the papain inhibitory assay. The cystatin consists of 111 amino acid residues with two disulfide linkages formed between 66-75 and 89-109, and has 43% identical sequences with chicken egg-white cystatin with consensus sequences of reactive sites, Gly(4), Gln-X-Val-X-Gly (48-52), and Ile(Val)-Pro-Trp (96-98).