The covalent structure of calf skin type III collagen. I. The amino acid sequence of the amino terminal region of the alpha 1(III) chain (position 1--222). 1979

P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn

The amino terminal 227 amino acid residues of the alpha 1(III) chain contain four CNBr peptides: alpha 1(III)CB3A (79 residues), CB3B, CB3C (6 residues each), CB7 (37 residues) and CB6 (99 residues). Fragmentation of the CNBr peptides was carried out using trypsin, chymotrypsin and the protease from Staphylococcus aureus V8. The fragments obtained were isolated by a combination of molecular sieve and ion exchange chromatography. The sequence analysis was performed according to the automated Edman degradation procedure.

UI MeSH Term Description Entries
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010447 Peptide Hydrolases Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D002918 Chymotrypsin A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side. Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D003094 Collagen A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH). Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012867 Skin The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.
D013211 Staphylococcus aureus Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications.
D014357 Trypsin A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. Tripcellim,Trypure,beta-Trypsin,beta Trypsin

Related Publications

P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
October 1983, The Biochemical journal,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
July 1979, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
October 1974, Biochimica et biophysica acta,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
October 1972, FEBS letters,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
July 1979, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
July 1979, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
July 1979, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
October 1972, FEBS letters,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
April 1980, Biochemistry,
P P Fietzek, and H Allmann, and J Rauterberg, and W Henkel, and E Wachter, and K Kühn
April 1981, Biochemistry,
Copied contents to your clipboard!