Structure and structure-function relationships in gonadotropins
نویسندگان
چکیده
منابع مشابه
Erythropoietin structure-function relationships.
In order to delineate functionally important domains in erythropoietin (Epo), we have prepared and tested a series of amino acid replacements at 51 conserved sites predicted to be on the surface of the molecule. Alanine replacements permitted preservation of a-helical structure. Wild type and mutant Epo cDNAs were transiently expressed at high levels in COS1 and COS7 cells. The biological activ...
متن کاملStructure–function relationships in calpains1
Calpains are a family of complex multi-domain intracellular enzymes that share a calcium-dependent cysteine protease core. These are not degradative enzymes, but instead carry out limited cleavage of target proteins in response to calcium signalling. Selective cutting of cytoskeletal proteins to facilitate cell migration is one such function. The two most abundant and extensively studied member...
متن کاملStructure-function relationships in dystrophin and utrophin.
Introduction The integrity of the animal cell membrane is believed to be maintained in part by the large (approx. 400 kDa) cytoskeletal proteins dystrophin and utrophin. Both proteins are capable of forming a link, probably flexible and potentially extensible/compressible, between the actin cytoskeleton and the cell membrane itself. Utrophin is expressed in all cell types, whereas dystrophin ex...
متن کاملStructure-Function Relationships of Phospholipases
In an effort to identify the anticoagulant region of venom phospholipases A2, we have systematically compared the amino acid sequences of strong, weak and non-anticoagulant phospholipases. The comparison disclosed several significant substitutions in the region between residues 54 and 77 (homology numbers). This proposed anticoagulant region is positively charged in strong, but negatively charg...
متن کاملPhycocyanin, cyanobacterial antioxidant: structure, function and applications
Phycobilins, open-chain tetrapyrrole pigment molecules, serve as accessory photosynthetic light-harvesting pigments in red algae and cyanobacteria. Phycobilin pigments are covalently linked with proteins and formed phycobiliproteins are organized into large macromolecular complexes called phycobilisomes on the top of the thylakoid membranes. In deep water, only green light is available, thus ph...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Reproduction Nutrition Développement
سال: 1988
ISSN: 0181-1916
DOI: 10.1051/rnd:19880201