sea/protease

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Diversity of the microbial community and cultivable protease-producing bacteria in the sediments of the Bohai Sea, Yellow Sea and South China Sea.

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The nitrogen (N) cycle is closely related to the stability of marine ecosystems. Microbial communities have been directly linked to marine N-cycling processes. However, systematic research on the bacterial community composition and diversity involved in N cycles in different seas is lacking. In this

Cortical granule proteases from sea urchin eggs.

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Developmentally regulated protease expression during sea urchin embryogenesis.

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A temporal study of protease expression employing the technique of SDS-PAGE gelatin substrate zymography revealed a definitive appearance of proteases during early development in the sea urchins, Lytechinus pictus and Strongylocentrotus purpuratus. The levels of these proteases increase

Genome sequence of the protease-producing bacterium Rheinheimera nanhaiensis E407-8T, isolated from deep-sea sediment of the South China Sea.

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The protease-producing bacterium E407-8(T) was isolated from deep-sea sediment of the South China Sea and has been identified recently as representing a new species, Rheinheimera nanhaiensis. The draft genome of R. nanhaiensis E407-8(T) consists of 3,987,205 bp and contains 3,730 predicated

Sea urchin eggs release protease activity at fertilization.

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Two high molecular mass proteases from sea urchin sperm.

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Two-types of high molecular mass proteases have been purified from sea urchin sperm using DEAE-Sephacel, hydroxylapatite and Superdex 200 column chromatography. Both proteases showed similar hydrolyzing activities toward synthetic peptides, but they differed in the molecular mass and peptide

Fertilization envelope assembly in sea urchin eggs inseminated in chloride-deficient sea water: II. Biochemical effects.

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Eggs of the sea urchin Strongylocentrotus purpuratus were fertilized in normal and in several chloride-deficient sea waters ([ Cl-]: normal greater than isethionate greater than methyl sulfonate greater than bromide). The fertilization envelopes (FE) were thinner and failed to harden, and the

Mitrochondrial and cytoplasmic protease activity in sea urchin eggs.

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Chymotrypsin-like proteases from the sea anemone, Metridium senile.

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Fungal life in the dead sea.

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The waters of the Dead Sea currently contain about 348 g/l salts (2 M Mg(2+), 0.5 M Ca(2+), 1.5 M Na(+), 0.2 M K(+), 6.5 M Cl(-), 0.1 M Br(-)). The pH is about 6.0. After rainy winters the surface waters become diluted, triggering development of microbial blooms. The 1980 and 1992 blooms were

Sea urchin protease specific to the SPKK motif in histone.

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A protease activity specific to spermatogenous histones was found in the egg extract of sea urchin. The enzyme responsible for this activity, named SPKK protease because of its substrate specificity, was purified as a monomeric 28 kDa protein. SPKK protease activity is inhibited by leupeptin and is

[Dynamics of ecological-biochemical characteristics of the sea ice in the coastal zone of the White sea].

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The distribution of salinity, silicon and phosphorus contents, and hydrolytic enzyme activities along a sea-coast transect was studied in melted ice cores and water samples taken from under the ice cover in the periods of active ice formation and melting in the Kandalaksha Bay, White Sea. The

Protease activity establishes the block against polyspermy in sea urchin eggs.

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Kunitz-type protease inhibitors from acrorhagi of three species of sea anemones.

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Sea anemones are rich in biologically active polypeptides such as toxins and protease inhibitors. These polypeptides have so far been isolated from whole bodies, tentacles or secreted mucus. Recently, two novel peptide toxins with crab lethality have been isolated from acrorhagi (specialized

Isolation of a protease from sea urchin eggs before and after fertilization.

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Upon fertilization, sea urchin eggs (Stronglyocentrotus pupuratus) release a protease into the surrounding sea water. This protease is in a particulate form which can be solubilized. The soluble form was purified by affinity chromatography on columns of immobilized soybean trypsin inhibitor. The

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