Protein amino acid lability

Soybean Protein Isolates. Soybean protein isolates, having a protein content of >90 wt%, are the only vegetable proteins that are widely used in imitation dairy products (1). Most isolates are derived from isoelectric precipitation, so that the soybean protein isolates have properties that are similar to those of casein. They are insoluble at thek isoelectric point, have a relatively high proportion of hydrophobic amino acid residues, and are calcium-sensitive. They differ from casein in that they are heat-denaturable and thus heat-labile. The proteins have relatively good nutritional properties and have been increasingly used as a principal source of protein. A main deterrent to use has been the beany flavor associated with the product. Use is expected to increase in part because of lower cost as compared to caseinates. There has been much research to develop improved soybean protein isolates. 

In contrast to the lability of certain dN adducts formed by the BHT metabolite above, amino acid and protein adducts formed by this metabolite were relatively stable.28,29 The thiol of cysteine reacted most rapidly in accord with its nucleophilic strength and was followed in reactivity by the a-amine common to all amino acids. This type of amine even reacted preferentially over the e-amine of lysine.28 In proteins, however, the e-amine of lysine and thiol of cysteine dominate reaction since the vast majority of a-amino groups are involved in peptide bonds. Other nucleophilic side chains such as the carboxylate of aspartate and glutamate and the imidazole of histidine may react as well, but their adducts are likely to be too labile to detect as suggested by the relative stability of QMs and the leaving group ability of the carboxylate and imidazole groups (see Section 9.2.3). 

Fukuoka was found to be homozygous for the 1615 G to A (539 Asp to Asn) mutation. This mutation occurred at relatively conserved amino acid residues and caused an alteration in hydrophobicity. Recently, we examined the structure-function relationship of these variants using the recombinant protein (F14). Although all of the four variants were found to be heat labile, the residual GPI activity seems to reflect clinical severity, such as the degree of anemia and episodes of hemolytic crisis. GPI Matsumoto, associated with severe anemia and hemolytic crisis, was extremely unstable, and GPI Iwate, which is associated with compensated hemolytic anemia, showed moderate heat instability. Affinity for substrate, fructose-6-phosphate, was slightly decreased in GPI Narita and GPI Fukuoka, which were associated with moderate anemia and hemolytic crisis. 

Rubredoxins do not have acid-labile sulfur as do ferredoxins, with the iron characterized by a mercaptide coordination. They are small proteins composed of some 50 amino acids. Both oxidized and reduced forms are high spin. 

Designing more stable enzyme proteins, e.g. via genetically replacing oxidation labile amino acids with more stable ones, has been followed for several other... 

The vast majority of research focused on selenium in biology (primarily in the fields of molecular biology, cell biology, and biochemistry) over the past 20 years has centered on identification and characterization of specific selenoproteins, or proteins that contain selenium in the form of selenocysteine. In addition, studies to determine the unique machinery necessary for incorporation of a nonstandard amino acid (L-selenocysteine) during translation also have been central to our understanding of how cells can utilize this metalloid. This process has been studied in bacterial models (primarily Escherichia colt) and more recently in mammals in vitro cell culture and animal models). In this work, we will review the biosynthesis of selenoproteins in bacterial systems, and only briefly review what is currently known about parallel pathways in mammals, since a comprehensive review in this area has been recently published. Moreover, we summarize the global picture of the nonspecific and specific use of selenium from a broader perspective, one that includes lesser known pathways for selenium utilization into modified nucleosides in tRNA and a labile selenium cofactor. We also review recent research on newly identified mammalian selenoproteins and discuss their role in mammalian cell biology. 

The isolation of an SCP protein from rat liver homogenates has also been reported (S2). This protein has been found to be heat-labile, to be detectable only in the liver, and to have a molecular weight of approximately 50,000 daltons by gel filtration (S2) and 28,000 daltons by sedimentation equilibrium (S3). Although the functional properties of the heat-labile SCP (SI) are similar to the heat-stable SCP (R2, R3), these proteins appear to be different. According to Scallen et al. (S3), their SCP preparation resembles chemically serum LDL this based on the similarity in amino acid composition between these two proteins. In the... 

Tyrosine (9-sulfate is stable under alkaline conditions, thus allowing for its quantification by amino acid analysis upon alkaline hydrolysis [0.2 M Ba(OH)2, 110 °C, 24 h] of sulfated tyrosine peptides and proteins.[6 331 Conversely, more than 95% of the ester is hydrolyzed after five minutes in 1M hydrogen chloride at 100 °C. Despite this pronounced acid lability, sulfated tyrosine peptides are sufficiently stable to short exposures of TFA134 35 or aqueous TFA[36 as required in peptide synthesis for removal of add-labile protecting groups. 

Protein hydrolysis in 6N HCl and subsequent analysis to determine amino acids (except tryptophan, which is acid labile) chemically present is a first step in protein quality evaluation. The chemical score and the EAA index represent attempts to use this information to chemically estimate nutritional quality of protein their obvious limitation is their disregard for amino acid availability. The chemical score is obtained by evaluating the percent of the limiting amino acid in comparison to that amino acid in whole egg protein ). The EAA index is the geometric mean of the ratios of each of the essential amino acids to those amino acids occurring in whole egg (4). 

---