The historic landscape of the Mendip Hills

When travelling north-east across the Somerset Levels and Moors the eye is drawn to the dark mass of the Mendip Hills, a Carboniferous Limestone ridge which rises abruptly from the flatness of its surroundings. The Historic Landscape of the Mendip Hills explores the archaeology and architecture of this remarkable corner of England, beginning with evidence for the first hunting groups who passed through the region over half a million years ago. Succeeding generations have left their mark on the Hills, from the enigmatic ceremonial structures of the Neolithic and Early Bronze Age, to the ancient farming landscapes and brooding hillforts of the Later Prehistoric period. Field archaeology, combined with architectural and historical enquiry, has also allowed a complex narrative to be constructed for more recent periods of history. This is a story dominated by adaptation and change, evidenced by the developing architecture of manorial centres and the shadowy remains of earlier structures fossilized within village houses. This volume presents a synthesis of the results of recent fieldwork undertaken by English Heritage and traces this region’s remarkable past, revealing ways in which it has shaped the landscape we see and value today.

OX133, a monoclonal antibody recognizing protein-bound N-ethylmaleimide for the identification of reduced disulfide bonds in proteins

In vivo, enzymatic reduction of some protein disulfide bonds, allosteric disulfide bonds, provides an important level of structural and functional regulation. The free cysteine residues generated can be labeled by maleimide reagents, including biotin derivatives, allowing the reduced protein to be detected or purified. During the screening of monoclonal antibodies for those specific for the reduced forms of proteins, we isolated OX133, a unique antibody that recognizes polypeptide resident, N-ethylmaleimide (NEM)-modified cysteine residues in a sequence-independent manner. OX133 offers an alternative to biotin-maleimide reagents for labeling reduced/alkylated antigens and capturing reduced/alkylated proteins with the advantage that NEM-modified proteins are more easily detected in mass spectrometry, and may be more easily recovered than is the case following capture with biotin based reagents.