scholarly journals Effect of acid hydrolysis on the racemization method using amino acid racemization in teeth.

1988 ◽  
Vol 37 (9) ◽  
pp. 476-480 ◽  
Author(s):  
Tsuneko OGINO ◽  
Hideki OGIUCHI ◽  
Toshiyuki HOBO ◽  
Hiroshi OGINO
1989 ◽  
Vol 54 (3) ◽  
pp. 803-810 ◽  
Author(s):  
Ivan Kluh ◽  
Ladislav Morávek ◽  
Manfred Pavlík

Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.


1972 ◽  
Vol 25 (10) ◽  
pp. 2139 ◽  
Author(s):  
M Stewart ◽  
CH Nicholls

The decomposition of tryptophan in aqueous HC1 at 100�C has been shown to proceed by a free-radical autoxidation mechanism. The acid functions by protonating the amino acid at either the 1- or 3-positions prior to autoxidation and so 1-methyltryptophan is also decomposed under these conditions. Impurities present in the soda glass containers used are shown to be responsible for the initiation of the reaction. The decomposition of tryptophan during the acid hydrolysis of proteins is considered in the light of these results.


2019 ◽  
Vol 50 ◽  
pp. 29-46 ◽  
Author(s):  
Marc R. Dickinson ◽  
Adrian M. Lister ◽  
Kirsty E.H. Penkman

2021 ◽  
Vol 6 (1) ◽  
pp. 32-41
Author(s):  
Purwantiningsih Sugita ◽  
Muhamad Rifai ◽  
Laksmi Ambarsari ◽  
Dyah Utami Cahyaning Rahayu ◽  
Hanhan Dianhar

Gelatin has been widely used as an additive in food industry pharmaceutical, and  cosmetic. The similar physical appearance between bovine and porcine gelatin causes an issue for some communities like a Muslim due to awareness of halal food. This study aims to produce gelatin from femur bones of bovines with acid hydrolysis and their characteristics compared to standard gelatin of bovine and porcine. Bovine and porcine bones were soaked in 5% HCl for 10 days and every 2 days a HCl solution was replaced to get ossein. Ossein is hydrolyzed by gradual heating at 65, 75, and 85oC. Gelatin  confirmed by  the physico-chemical characters, FT-IR and analysis amino acid with HPLC.The results showed that the yield of bovine gelatin was 4.33%. The physico-chemical characters of bovine gelatin resulting from isolation and bovine gelatin standards are in conformity with porcine gelatin standards and meet the requirements of SNI 06-3735-1995 and GMIA. Therefore, bovine gelatin is specifically capable of substituting porcine gelatin for application in the pharmaceutical field. The FTIR spectrum of bovine gelatin shows the presence of amide A, amide I, amide II and amide III groups. The amino acid characters of gelatin were identified as glycine (13.57%) and proline (1.62%) for bovine gelatin and glycine (0.51%) and proline (0.09%) for porcine gelatin.


Author(s):  
Shu-jane Shen ◽  
Heinz G. Floss ◽  
Hidehiko Kumagai ◽  
Hideaki Yamada ◽  
Nobuyoshi Esaki Kenji Soda ◽  
...  

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