PMID: 6526384

 

    Legend: Gene, Sites

Title : [The primary structure of human free secretory component and the arrangement of disulfide bonds]

Abstract :

1. The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry
2. The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine
3. The protein contains 20 cysteine residues but, as a special feature, no methionine
4. The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length
5. The 20 cysteine residues form 10 disulfide bonds, 9 of which confirm the internal homology by their characteristic arrangement
6. The free secretory component also shows homology to immunoglobulins in some sections
7. A computer-supported tertiary structure is proposed for the free secretory component

Output (sent_index, trigger, protein, sugar, site):

• 2. glycoprotein, , glycoprotein, -, -

Output(Part-Of) (sent_index, protein, site):

• 3. protein, cysteine residues

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX