The effects of strength, aerobic, and concurrent exercise on skeletal muscle damage in rats.

Introduction: In this study we examined oxidative stress and skeletal muscle damage resulting from acute strength, aerobic, or concurrent exercise in rats.

Methods: The animals were divided into control (C), strength (SE), aerobic (AE), and combined (CE) exercise groups. They were euthanized at 3 different time-points (6, 24, and 48 h) after acute exercise.

Biological activities of ACL-I and physicochemical properties of ACL-II, lectins isolated from the marine sponge Axinella corrugata.

Lectin II from the marine sponge Axinella corrugata (ACL-II) was purified by affinity chromatography on rabbit erythrocytic stroma incorporated into a polyacrylamide gel, followed by gel filtration on Ultrogel AcA 44 column. Purified ACL-II is a lectin with an Mr of 80 kDa and 78 kDa, estimated by SDS-PAGE and by FPLC on Superose 12 HR column, respectively. ACL-II mainly agglutinates native rabbit erythrocytes and this hemagglutinating activity is independent of Ca(2+), Mg(2+) and Mn(2+), but is inhibited by d-galactose, chitin and N-acetyl derivatives, with the exception of GalNAc.

Immunohistochemical localization of an N-acetyl amino-carbohydrate specific lectin (ACL-I) of the marine sponge Axinella corrugata.

The N-acetyl amino-carbohydrate specific lectin (ACL-I) was previously identified and purified by us from the marine sponge Axinella corrugata (phylum Porifera, class Demospongiae). The distribution of the specific lectin within the tissue of the sponge was studied by bright-field optical microscopy immunohistochemistry in order to better understand its physiological role in the sponge. Polyclonal antibodies were raised against purified ACL-I in mice and tested by Western blot technique.

ACL-I, a lectin from the marine sponge Axinella corrugata: isolation, characterization and chemotactic activity.

The lectin from the marine sponge Axinella corrugata (ACL-I) was purified by affinity chromatography on rabbit erythrocytic stroma incorporated into a polyacrylamide gel followed by gel filtration on Ultrogel AcA 44 column. Purified ACL-I is a hexameric glycoprotein with a Mr of 82.3 kDa estimated by SDS-PAGE and 78.

Fine carbohydrate recognition of Euphorbia milii lectin.

Glycans are key structures involved in biological processes such as cell attachment, migration, and invasion. Information coded on cell-surface glycans is frequently deciphered by proteins, as lectins, that recognize specific carbohydrate topology. Here, we describe the fine carbohydrate specificity of Euphorbia milii lectin (EML).