calsequestrin/spinacia

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Evidence that spinach leaves express calreticulin but not calsequestrin.

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Ingia / Ingia

The presence of either calreticulin (CR) or calsequestrin (CS-like proteins in spinach (Spinacia oleracea L.) leaves has been previously described. Here we report the purification from spinach leaves of two highly acidic (isoelectric point 5.2) Ca(2+)-binding proteins of 56 and 54 kD by means of

Plant cells contain calsequestrin.

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Ingia / Ingia

Calsequestrin is a high capacity low affinity Ca2+-binding protein thought to be essential for the function of the intracellular rapid releasable Ca2+ pool of a variety of animal cells. Here we show that two types of plant tissues, cultured Streptanthus tortuosus cells and spinach leaves, contain a

Calreticulin is the major Ca2+ storage protein in the endoplasmic reticulum of the pea plant (Pisum sativum).

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala

Ingia / Ingia

A 56kDa protein with high similarity in its N-terminal amino acid sequence to animal calreticulin and 100% homology with the N-terminal amino acids of spinach calreticulin has been identified in seeds of the pea plant (Pisum sativum). A new purification procedure is described by which the

Purification of calreticulin-like protein(s) from spinach leaves.

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala

Ingia / Ingia

In a search for the plant equivalent of calsequestrin or calreticulin, the high capacity, low affinity Ca2+ binding proteins of muscle and non-muscle cells thought to play important roles in Ca2+ storage, we purified two Ca(2+)-binding proteins from spinach leaves. The proteins had apparent

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Herbal & Natural Medicine

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