Ligand-stabilized Conformations in Serum Albumin

Markus, Gabor; McClintock, David K.; Castellani, Barbara A.

doi:10.1016/s0021-9258(18)99553-0

Cited by 47 publications

(9 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, either the aromatic amino acid composition of the fragments is altered when digestion is performed in the presence of Ca2+, or the splitting of ~12 bonds under these conditions is less efficient in producing fragment L, pre-A, A, and B than it is in its absence. This is similar to what has been found for Methyl Orange (Markus et al, 1967b).…”

Section: Resultssupporting

confidence: 91%

“…The amount of alkali consumed by neutralization of the trypsin is obtained by extrapolation of the curve back to zero time over the short 24-sec time interval. In many instances, when the reaction had slowed down considerably, the reaction mixture was titrated rapidly to pH 9.0 so as to obtain a factor (1.19) whereby equivalents of alkali consumed could be converted to bonds split (Markus et al, 1967b).…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Influence of steroid binding on the tryptic hydrolysis of serum albumin

Ryan¹

1973

Biochemistry

View full text Add to dashboard Cite

Section: Resultssupporting

confidence: 91%

Section: Methodsmentioning

confidence: 99%

Influence of steroid binding on the tryptic hydrolysis of serum albumin

Ryan¹

1973

Biochemistry

View full text Add to dashboard Cite

“…The rationale for the digestion of albumin bound to palmityl-agarose is that coupling of a tightly bound ligand protects a portion of the protein against proteolysis (Markus et al, 1967a). Digestion of albumin which is immobilized by coupling to fatty acyl-agarose should thus offer a means of obtaining fragments containing primary fatty acid binding sites; it has the advantage that residual trypsin is removed during the washing procedure before elution of the remaining, trypsin-resistant portion of the molecule (Figure 1).…”

Section: Resultsmentioning

confidence: 99%

Purification and properties of fragments of bovine serum albumin. I. Fragments of bovine serum albumin produced by limited proteolysis. Isolation and characterization of tryptic fragments

Peters¹,

Feldhoff²

1975

Biochemistry

View full text Add to dashboard Cite

Several fragments of bovine serum albumin have been isolated following limited tryptic hydrolysis and their positions then determined in the bovine serum albumin sequence published by J. R. Brown ((1975), Fed. Proc., Fed. Am. Soc. Exp. Biol. 34, 591). When bovine serum albumin was coupled to palmityl-aminoethylamino-agarose and digested with trypsin, two fragments were obtained: (a) peptide 115-184, containing the highly aromatic disulfide loop 3 of Brown's model, and (b) a larger fragment, residues 377-581, containing disulfide loops 7-9. This fragment constitutes the third of the three domains of the albumin molecule. From bovine serum albumin digested in solution, peptide 115-184 was again obtained, as well as (c) a 39,000-dalton fragment identified as residues 198-581, loops 4-9 of the second and third domains, but with a long, tryptophan-containing segment 204-238 missing from loop 4. The ability to isolate these fragments without cleaving disulfide bridges is partial confirmation of the proposed model of bovine serum albumin as a series of nine independent loops.

show abstract

“…Protein conformation may be affected by ligand binding, which may alter proteolytic susceptibility 94 , 95 . Earlier studies have shown this characteristic of proteins, namely, proteins, tends to be more resistant to proteolysis when bound to a ligand 96 , 97 . Based on the limited proteolysis susceptibility shift of protein targets, label-free drug protein target identification strategies, such as DARTS, were first proposed 30 .…”

Section: Direct Screening Strategies Based On the Differential Limite...mentioning

confidence: 93%

An update of label-free protein target identification methods for natural active products

Cui¹,

Li²,

Chen³

et al. 2022

Theranostics

View full text Add to dashboard Cite

Natural active products (NAPs) are derived from chemical substances found in nature that have biological activity and medicinal potential. Screening and revealing the protein targets of NAPs is an indispensable link in the pharmacological and toxicological understanding of NAPs. Proteins are the main factors executing cell functions, and cells rely on the function of proteins to complete various activities in the life cycle. The important mechanism of action of drugs is to regulate cell biological activities by interacting with proteins and other macromolecules. At present, the classic way to screen protein targets is based on the molecular label tracing method, which has a long cycle and changes the molecular structure and pharmacological effects of NAPs. Due to the shortcomings of molecular labelling methods, in recent years, scientists have tried to develop a variety of label-free protein target identification methods for NAPs and have made a certain amount of progress. This article reviews the current protein target identification methods for NAPs with the aim of providing a reference for research on NAP protein targets.

show abstract

Ligand-stabilized Conformations in Serum Albumin

Cited by 47 publications

References 13 publications

Influence of steroid binding on the tryptic hydrolysis of serum albumin

Influence of steroid binding on the tryptic hydrolysis of serum albumin

Purification and properties of fragments of bovine serum albumin. I. Fragments of bovine serum albumin produced by limited proteolysis. Isolation and characterization of tryptic fragments

An update of label-free protein target identification methods for natural active products

Contact Info

Product

Resources

About