Purification and Some of the Properties of αs-Casein and κ-Casein

Zittle, Charles A.; Custer, J.H.

doi:10.3168/jds.s0022-0302(63)89242-5

Cited by 342 publications

(82 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…'O) IX" -Casein was prepared from fresh cows' milk by the method of Zittle and Custer. 14) Other chemicals were extra-pure reagents from Wako Pure Chemicals Co.…”

Section: Methodsmentioning

confidence: 99%

Gelation Mechanism of Protein Solution by Transglutaminase

Nio

Motoki

Takinami

1986

Agricultural and Biological Chemistry

View full text Add to dashboard Cite

“…'O) IX" -Casein was prepared from fresh cows' milk by the method of Zittle and Custer. 14) Other chemicals were extra-pure reagents from Wako Pure Chemicals Co.…”

Section: Methodsmentioning

confidence: 99%

Gelation Mechanism of Protein Solution by Transglutaminase

Nio

Motoki

Takinami

1986

Agricultural and Biological Chemistry

View full text Add to dashboard Cite

“…15 ) Soybean 11 Sand 7S globulins were prepared from def atted soybean flour (Ajinomoto Co., Inc.) by the method of Thanh et al 16 ) Other chemicals were extra pure reagents from Wako Pure Chemicals, Co.…”

Section: Methodsmentioning

confidence: 99%

Gelation of Casein and Soybean Globulins by Transglutaminase

Nio

Motoki

Takinami

1985

Agricultural and Biological Chemistry

View full text Add to dashboard Cite

“…Substrates xA-casein was prepared according to Zittle and Custer [9], from the milk of a single cow (FranGaise-Frisonne Pie Noire breed) homozygous at the ;K CnA locus.…”

Section: Enzymesmentioning

confidence: 99%

Purification and Characterization of Bovine Gastricsin

Martin

Trieu‐Cuot

Collin

et al. 1982

European Journal of Biochemistry

View full text Add to dashboard Cite

The results reported in the present paper and N-terminal sequence homologies established by other authors strongly support the assumption that the gastric protease previously called bovine pepsin I or bovine pepsin B belongs to the aspartate protease group and corresponds to gastricsin (or pepsin C) (EC 3.4.23.3) from other species.Bovine gastricsin was prepared from commercial extracts of adult bovine vells by a procedure involving DEAE-cellulose chromatography, gel filtration on Sephacryl S-200 and a further DEAE-cellulose chromatography. The preparation thus obtained was shown to be free of chymosin and bovine pepsin A by immunodiffusion, selective inactivation in urea and isoelectric focusing. Its molecular weight was estimated by gel filtration to be 32 800.Bovine gastricsin displayed microheterogeneity on isoelectric focusing with pl values of the components ranging from 3.5 to 4.0. Chromatography of bovine gastricsin on hydroxyapatite separated three fractions, none of them being homogeneous by isoelectric focusing. Concanavalin-A-Sepharose 4B bound bovine gastricsin to some extent, but without any significant fractionation. Proteolytic activity could be detected directly on the isoelectric focusing gel for all the components of gastricsin and its fractions from hydroxyapatite and concanavalin-A -Sepharose 4B.Bovine gastricsin and its fractions from hydroxyapatite have similar amino acid compositions, different from those of bovine chymosin and pepsin A but obviously related to those of human, simian and porcine gastricsins.Bovine gastricsin which is inactivated by reaction with diazoacetyl-~~-nor~eucine methyl ester and with 1,2-epoxy-(p-nitrophenoxy)propane in a 1 : I and 1 : 2 stoichiometry, respectively, is able to hydrolyse a synthetic hexapeptide, Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OMe, used as reference substrate for aspartate proteases, and exhibits a low activity towards N-acetyl-L-phenylalanyl-L-diiodotyrosine. Its specific clotting activity with x-casein as substrate is only half of that of chymosin and pepsin A.

show abstract

Purification and Some of the Properties of αs-Casein and κ-Casein

Cited by 342 publications

References 15 publications

Gelation Mechanism of Protein Solution by Transglutaminase

Gelation Mechanism of Protein Solution by Transglutaminase

Gelation of Casein and Soybean Globulins by Transglutaminase

Purification and Characterization of Bovine Gastricsin

Contact Info

Product

Resources

About