alpha-chymotrypsin and Seizures

alpha-chymotrypsin has been researched along with Seizures* in 2 studies

Other Studies

2 other study(ies) available for alpha-chymotrypsin and Seizures

Article	Year
Monoiodoinsulin. Preparation, purification, and characterization of a biologically active derivative substituted predominantly on tyrosine A14. The Journal of biological chemistry, 1974, Jan-10, Volume: 249, Issue:1 Topics: Amino Acid Sequence; Animals; Biological Assay; Blood Glucose; Cattle; Chromatography, Ion Exchange; Chymotrypsin; Circular Dichroism; Diabetes Mellitus, Experimental; Electrophoresis, Polyacrylamide Gel; Guinea Pigs; Hemolysis; Hydrogen-Ion Concentration; Insulin; Insulin Antibodies; Iodine; Iodine Radioisotopes; Mice; Mice, Inbred C57BL; Oxidation-Reduction; Radioimmunoassay; Seizures; Spectrophotometry, Ultraviolet; Sulfites; Tyrosine	1974
Porcine proinsulin: characterization and amino acid sequence. Science (New York, N.Y.), 1968, Jul-12, Volume: 161, Issue:3837 Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin. A molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies. Through the action of trypsin this single-chain protein is transformed to desalanine insulin by cleavage of a polypeptide chain connecting the carboxy-terminus of the B chain to the amino-terminus of the A chain of insulin. The amino acid sequence of this connecting peptide was found to be Arg-Arg-Glu-Ala-Gln-Asn-Pro-Gln-Ala-Gly-Ala-Val-Glu-Leu-Gly-Gly-Gly-Leu-Gly-Gly-Leu-Gln-Ala-Leu-Ala-Leu-Glu-Gly-Pro-Pro-Gln-Lys-Arg. Topics: Amino Acid Sequence; Animals; Biological Assay; Cellulose; Chromatography, Ion Exchange; Chymotrypsin; Electrophoresis, Disc; Hypoglycemia; Insulin; Molecular Weight; Peptides; Proteins; Seizures; Swine; Trypsin	1968

Article

Year

Monoiodoinsulin. Preparation, purification, and characterization of a biologically active derivative substituted predominantly on tyrosine A14.

The Journal of biological chemistry, 1974, Jan-10, Volume: 249, Issue:1

Topics: Amino Acid Sequence; Animals; Biological Assay; Blood Glucose; Cattle; Chromatography, Ion Exchange; Chymotrypsin; Circular Dichroism; Diabetes Mellitus, Experimental; Electrophoresis, Polyacrylamide Gel; Guinea Pigs; Hemolysis; Hydrogen-Ion Concentration; Insulin; Insulin Antibodies; Iodine; Iodine Radioisotopes; Mice; Mice, Inbred C57BL; Oxidation-Reduction; Radioimmunoassay; Seizures; Spectrophotometry, Ultraviolet; Sulfites; Tyrosine

1974

Porcine proinsulin: characterization and amino acid sequence.

Science (New York, N.Y.), 1968, Jul-12, Volume: 161, Issue:3837

Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin. A molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies. Through the action of trypsin this single-chain protein is transformed to desalanine insulin by cleavage of a polypeptide chain connecting the carboxy-terminus of the B chain to the amino-terminus of the A chain of insulin. The amino acid sequence of this connecting peptide was found to be Arg-Arg-Glu-Ala-Gln-Asn-Pro-Gln-Ala-Gly-Ala-Val-Glu-Leu-Gly-Gly-Gly-Leu-Gly-Gly-Leu-Gln-Ala-Leu-Ala-Leu-Glu-Gly-Pro-Pro-Gln-Lys-Arg.

Topics: Amino Acid Sequence; Animals; Biological Assay; Cellulose; Chromatography, Ion Exchange; Chymotrypsin; Electrophoresis, Disc; Hypoglycemia; Insulin; Molecular Weight; Peptides; Proteins; Seizures; Swine; Trypsin

1968