Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
2001-6-25
pubmed:abstractText
Penaeus monodon (class Crustacea, order Decapoda) is one of the largest shrimps of the Penaeidea family from the Indo-West Pacific region. The dioxygen-transporting protein hemocyanin, isolated from the hemolymph of this invertebrate, is composed of three 75-76 kDa structural/functional subunits designated as Pm1, Pm2 and Pm3. The N-terminal sequences of the chains were determined and compared with those of other decapodan hemocyanin subunits. Pm2 and Pm3 are highly homologous and electrophoretically undistinguishable polypeptides. In comparison to Pml, they have an extension of six residues. Pm1 is closely related to the subunit Pv2 of the Penaeus vannamei hemocyanin. Probably, subunits like Pm1 and Pv2 are family-specific for the Penaeidea hemocyanins and the other subunits are species-specific. Comparison of N-terminal sequences of respiratory proteins from the sub-orders Natantia and Reptantia demonstrated family- and sub-order-specific sequences. A melting point of 69 degrees C, lower than those for the di-hexameric decapodan hemocyanins, was determined from the temperature dependence of ellipticity of the mono-hexameric Penaeus monodon hemocyanin. Thermostability of decapodan hemocyanins depends on their aggregation state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0939-5075
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
416-22
pubmed:dateRevised
2009-11-4
pubmed:meshHeading
pubmed:articleTitle
Penaeus monodon (tiger shrimp) hemocyanin: subunit composition and thermostability.
pubmed:affiliation
Abteilung für Physikalische Biochemie, Physiologisch-chemisches Institut der Universität Tübingen, Germany. stanka.stoeva@uni-tubingen.de
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't