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Topic:Proteomics

Proteomics is the large-scale study of proteins, particularly their structures and functions, in horses. This field encompasses the analysis of the complete set of proteins expressed by the equine genome, known as the proteome. Proteomics research in horses aims to understand the diverse roles of proteins in various biological processes, including growth, development, and response to environmental stimuli. Techniques such as mass spectrometry and protein microarrays are commonly employed to identify and quantify proteins, assess post-translational modifications, and investigate protein-protein interactions. This page compiles peer-reviewed research studies and scholarly articles that explore the methodologies, findings, and implications of proteomics in equine health and disease.
The amino acid sequence of equine alpha-lactalbumin.
Biochemistry international    November 1, 1984   Volume 9, Issue 5 539-546 
Kaminogawa S, McKenzie HA, Shaw DC.The amino acid sequence of equine alpha-lactalbumin has been determined with the aid of an automatic sequencer. The protein chain consists of 123 amino acids and has a Mr of 14218. Elucidation of the structure involved sequence determination of native protein (residues 1-32), cyanogen bromide fragments, and tryptic, chymotryptic and S. aureus V8 proteolytic peptides. Approximately 67% of the residues are identical with corresponding residues of bovine alpha-lactalbumin B, and there is close homology with alpha-lactalbumin of other species.
Natural protease inhibitors: qualitative and quantitative assay by fibrinogen-agarose electrophoresis.
Analytical biochemistry    May 1, 1984   Volume 138, Issue 2 335-339 doi: 10.1016/0003-2697(84)90818-2
Pellegrini A, Hägeli G, Fretz D, von Fellenberg R.An electrophoretic procedure for the qualitative and quantitative assay of protein protease inhibitors is reported. This assay is particularly suited for investigations of crude biological materials when specific antisera are not available. The supporting medium consists of agarose into which denatured fibrinogen is incorporated as the substrate for proteases. The processing then is divided into two steps: (1) electrophoretic resolution of the inhibitor containing material and (2) detection of the inhibitor bands through their protease inhibiting activity. The inhibitor position is thus made v...
Characterisation of glycoproteins in the sweat of the horse (Equus caballus).
Research in veterinary science    March 1, 1984   Volume 36, Issue 2 231-234 
Eckersall PD, Beeley JG, Snow DH, Thomas A.The two major polypeptides H (Mr 49,000) and L (Mr 33,000) of equine sweat have been purified by gel filtration and characterised by gel electrophoresis and compositional analysis. Both H and L are glycoproteins containing sialic acid, neutral sugars, N-acetylglucosamine and N-acetylgalactosamine, but the two polypeptides differ considerably in the extent of glycosylation. H and L also differ in amino acid composition, but both contain only low levels of sulphur containing amino acids and histidine. These glycoproteins may behave as surfactants.
Studies on the nature of the equine protease inhibitors.
Animal blood groups and biochemical genetics    January 1, 1984   Volume 15, Issue 2 151-154 doi: 10.1111/j.1365-2052.1984.tb01111.x
Ek N, Braend M.No abstract available
Two-dimensional electrophoresis of horse serum proteins: genetic polymorphism of ceruloplasmin and two other serum proteins.
Animal blood groups and biochemical genetics    January 1, 1984   Volume 15, Issue 4 237-250 doi: 10.1111/j.1365-2052.1984.tb01124.x
Juneja RK, Andersson L, Sandberg K, Gahne B, Adalsteinsson S, Gunnarsson E.Two-dimensional agarose gel (pH 8.6)-horizontal polyacrylamide gel (pH 9.0) electrophoresis of horse serum proteins revealed genetic polymorphism of ceruloplasmin (Cp) and two unidentified serum proteins tentatively designated serum protein 1 (SP1) and serum protein 2 (SP2). Family data were consistent with the hypothesis that the observed Cp and SP1 phenotypes were each controlled by two codominant, autosomal alleles. The three common SP2 phenotypes were shown to be controlled by two codominant, autosomal alleles. Population data and limited family data indicated the occurrence of two additio...
Synthesis and properties of equine beta-melanotropin analogs with substitution in residue position 1.
International journal of peptide and protein research    April 1, 1983   Volume 21, Issue 4 364-368 doi: 10.1111/j.1399-3011.1983.tb03116.x
Nádasdi L, Yamashiro D, Li CH, Izdebski J.Five analogs of equine β-melanotropin have been synthesized by the solid phase method. The NH2-terminal aspartic acid was substituted with amino acids (Gly, Trp, Ile, Lys and Nα-acetyl-Asp) differing widely in physicochemical properties. On the basis of their lipolytic potencies it was concluded that this position plays a negligible role in this activity.
Simultaneous isolation and partial characterization of antithrombin III and alpha 1-proteinase inhibitor from horse plasma.
Acta biochimica Polonica    January 1, 1982   Volume 29, Issue 1-2 95-103 
Kurdowska A, Koj A, Jaśkowska M.No abstract available
Interactions of different albumins and animal sera with insolubilized Cibacron Blue, Evaluation of apparent affinity constants.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1982   Volume 71, Issue 3 403-407 doi: 10.1016/0305-0491(82)90401-1
Naval J, Calvo M, Lampreave F, Piñeiro A.1. A high concentration Cibacron Blue-Sepharose derivative has been used to study the affinity chromatography of albumin from eight animal species. 2. The apparent affinity constants for albumin varies between 3.9 x 10(4) M-1 and 0.9 x 10(4) M-1, in the order: Human greater than rabbit greater than horse greater than pig = dog greater than bovine greater than rat greater than chicken. 3. Other serum proteins were also bound to the gel, particularly lipoproteins and alpha 2-macroglobulin.
Primary structure of 3-phosphoglycerate kinase from horse muscle. I. Purification of cyanogen bromide peptides and amino acid sequence of peptide CB5 (104 residues).
The Journal of biological chemistry    October 25, 1981   Volume 256, Issue 20 10284-10292 
Hardy GW, Darbre A, Merrett M.3-Phosphoglycerate kinase was isolated from horse muscle and subjected to the action of cyanogen bromide. The resulting peptides were separated using gel filtration combined with either ion exchange chromatography on phosphocellulose in 6 M urea or high voltage paper electrophoresis. The sequence of the largest peptide, CB5, has been determined by a combination of automated and manual Edman degradation carried out on the intact peptide and derivatives obtained by proteolytic digestion. The isolation of two peptides derived from CB5 by cleavage of the bond between Asp109 and Pro110 facilitated ...
Stabilization of the C-terminal part of pig and horse colipase by carboxypeptidase and trypsin inhibitors.
European journal of biochemistry    March 16, 1981   Volume 115, Issue 1 99-105 doi: 10.1111/j.1432-1033.1981.tb06203.x
Chapus C, Desnuelle P, Foglizzo E.Pig and horse colipases have been purified by a common procedure using trypsin and carboxypeptidase inhibitors as stabilizers. Two forms of pig colipase were identified: a predominant A1 form with about 103-105 residues, and a minor slightly degraded A2 form in which the last two C-terminal residues, Asp and Ser, were lacking. This type of degradation is considerably slowed down by carboxypeptidase inhibitors. A total of four forms of the horse cofactor were characterized: two (A1 and B1) were probably isocolipases which differed by only a few substitutions. Both contained the same number of r...
The cleavage of the Met-Lys bond in a bradykinin derivative by glandular kallikreins.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    March 1, 1981   Volume 362, Issue 3 337-345 doi: 10.1515/bchm2.1981.362.1.337
Araujo-Viel MS, Juliano L, Prado ES.The synthetic tridecapeptide Gly-Leu-Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg was used as a model substrate for horse urinary and porcine pancreatic kallikreins. The Met-Lys bond is hydrolyzed selectively by both enzymes. Oxidation of the methionine residue to sulfoxide made the peptide resistant to both kallikreins. Substitution of either the methionine or lysine residues by norleucine led to peptides in which the Nle-Lys or the Met-Nle bonds, respectively, were susceptible to the urinary kallikrein. The esterolytic and Met-Lys bond-splitting activities of both enzymes were inhibited simil...
Biochemical properties of equine chorionic gonadotrophin from two different pools of pregnant mare sera.
Biology of reproduction    October 1, 1980   Volume 23, Issue 3 570-576 doi: 10.1095/biolreprod23.3.570
Aggarwal BB, Farmer SW, Papkoff H, Seidel GE.No abstract available
Protease inhibitor system in horses: classification and detection of a new allele.
Animal blood groups and biochemical genetics    January 1, 1980   Volume 11, Issue 4 235-244 doi: 10.1111/j.1365-2052.1980.tb01514.x
Pollitt CC, Bell K.A method of horizontal thin layer polyacrylamide gel electrophoresis at acid pH has been developed for the separation of the prealbumins in equine plasma. Using this method, it has been possible to split the S allele into two, S1 and S2, bringing the total number of prealbumin alleles in Thoroughbred horses to eight. The gene frequencies of these eight alleles in Australian Thoroughbreds are presented. All eight prealbumin types exhibit antiprotease activity and therefore, it is suggested that the name prealbumin (Pr) should be abandoned in favour of protease inhibitor (Pi) although at this st...
Occurrence of Leu-Lys-bradykinin and histidine-rich peptide in high-molecular-weight kininogen isolated from horse plasma.
Biochimica et biophysica acta    August 28, 1979   Volume 579, Issue 2 474-478 doi: 10.1016/0005-2795(79)90076-x
Sugo T, Kato H, Iwanaga S, Fujii S.On incubation of purified horse plasma high-molecular-weight kininogen with purified plasma kallikrein, three new peptides, named fragment 1.2, fragment 1 and fragment 2, were released, in addition to the vasopeptide, bradykinin. Fragment 2 contained an extremely high level of histidine, in which eleven residues out of the total 48 residues were characterized. Thus the result proves the existence of the histidine-rich region in horse high-molecular-weight kininogen, which is similar to the region previously identified in bovine high-molecular-weight kininogen. Moreover, we have identified a ne...
The effect of binding ions on the oxidation of horse heart ferrocytochrome c.
Canadian journal of biochemistry    May 1, 1979   Volume 57, Issue 5 372-377 doi: 10.1139/o79-047
Peterman BF, Morton RA.The research explores how different binding ions affect the oxidation speed of horse heart ferrocytochrome c, a protein, by potassium ferricyanide at a constant ionic strength. Studying the Ion Effect […]
Specific reaction of aloe extract with serum proteins of various animals.
Experientia    April 15, 1978   Volume 34, Issue 4 523-524 doi: 10.1007/BF01935968
Fujita K, Suzuki I, Ochiai J, Shinpo K, Inoue S, Saito H.We found that aloe extract contains a lectin-like substance which reacts with serum proteins of various animals. Furthermore, in human serum 2 proteins, alpha2-macroglobulin and alpha1-antitrypsin, were shown to be reactive with aloe extract.
Studies on cytochrome c. XIV. Synthesis of the protected heptadecapeptide (sequence 88-104) of horse heart cytochrome c.
International journal of peptide and protein research    January 1, 1977   Volume 10, Issue 2 95-101 
Borin G, Filippi B, Cavaggion F, Marchiori F.A solution synthesis is described of the partially protected N alpha-benzyloxycarbonylheptadecapeptide Z-Lys (Tfa)-Thr-Glu-Arg-Glu-Asp-Leu-Ile-Ala-Tyr-Leu-Lys (Tfa)-Lys (Tfa)-Ala-Thr-Asn-Glu (OBu t)-OBu t corresponding to sequence 88-104 of horse heart cytochrome c. The synthesis is achieved through the preparation of two subunits H1 (sequence 88-96) and H2 (sequence 97-104) and their linkage by an azide coupling step.
Studies on cytochrome C. XIII. Synthesis of the protected undecapeptide (sequence 77-87) of horse heart cytochrome c.
International journal of peptide and protein research    January 1, 1977   Volume 10, Issue 2 89-94 
Borin G, Filippi B, Stivanello D, Marchiori F.A solution synthesis of Z-Gly-Thr-Lys (Tfa)-Met-Ile-Phe-Ala-Gly-Ile-Lys (Tfa)-Lys (Tfa)-NHNH-Boc corresponding to the sequence 77-87 of horse heart cytochrome c is described. The protected undecapeptide was obtained from intermediate hepta- and tetrapeptide fragments by an azide coupling.
Active-site labelling of kallikreins by chloromethylketone derivatives.
General pharmacology    August 1, 1976   Volume 7, Issue 2-3 163-166 doi: 10.1016/0306-3623(76)90055-0
Sampaio CA, Prado ES.Ala-Phe-Lys-CH2-Cl is a chloromethylketone derivative which is able to promote the inhibition of several proteolytic enzymes. In this paper the inhibition of horse urinary and plasmatic kallikreins is described and this inhibition is compared to that produced in human plasma kallikrein. This compound was designed based upon the structure of bradykinin. This enzyme substrate system can provide a model for the study of the interactions between bradykinin and its receptor. The inhibition of the enzymes was achieved both for its esterase and kinin-releasing activities.
Sweat proteins.
The British journal of dermatology    February 1, 1974   Volume 90, Issue 2 175-181 doi: 10.1111/j.1365-2133.1974.tb06382.x
Jenkinson DM, Mabon RM, Manson W.No abstract available
The biochemistry of ferritin.
British journal of haematology    June 1, 1973   Volume 24, Issue 6 677-680 doi: 10.1111/j.1365-2141.1973.tb01695.x
Crichton RR.The researchers investigated the biochemical properties of ferritin, a protein responsible for iron storage in the body. They identified its distribution and structure, noting variations in different species and tissues. […]
[Lipoproteins of various experimental animals].
Saishin igaku. Modern medicine    March 1, 1972   Volume 27, Issue 3 482-490 
Nagase S.No abstract available
Limited proteolysis of horse heart cytochrome c.
European journal of biochemistry    June 11, 1971   Volume 20, Issue 3 414-419 doi: 10.1111/j.1432-1033.1971.tb01407.x
Schejter A, Goldkorn T, Sokolovsky M.No abstract available
N-Terminal sequences of equine and human immunoglobulin heavy chains.
Biochimica et biophysica acta    February 17, 1970   Volume 200, Issue 2 258-266 doi: 10.1016/0005-2795(70)90169-8
Montgomery PC, Bello AC, Rockey JH.N-terminal tetrapeptides from heavy chains of equine γGab- and γT-globulins, and of human γG and γA myeloma proteins and a γM macroglobulin, have been studied. The equine and human heavy chains lacked free α-amino-terminal groups. After mild alkaline hydrolysis, glutamic acid was identified as the terminal amino acid by reaction with dimethylaminonaphthalenesulfonyl chloride, tentatively identifying pyrrolid-2-one-5-carboxylic acid (PCA) as the unreactive terminal residue of each heavy chain. Peptides lacking a free α-amino group were isolated from subtilisin and pronase digests of the ...
A comparison of fingerprints of tryptic digests of human, horse and rat apoferritins.
Comparative biochemistry and physiology    February 1, 1970   Volume 32, Issue 3 451-458 doi: 10.1016/0010-406x(70)90462-7
Richter GW, Moppert GA, Lee JC.1. Fingerprints of tryptic digests of apoferritins from a human liver, horse spleens and ACI rat livers were made by means of electrophoresis and chromatography on microcrystalline cellulose, and were compared. 2. All tryptic peptides also present in apoferritins from the human liver and the horse spleens were also present in apoferritin from the rat livers. 3. In the digests of horse and of rat apoferritin there was a peptide that was not present in the digests of human apoferritin. Another peptide was obtained from human and from rat apoferritin, but not from horse apoferritin. 4. T...
Gene expression in an interspecific hybrid: analysis of hemoglobins in donkey, horse, and mule by peptide mapping.
Biochemical genetics    February 1, 1970   Volume 4, Issue 1 73-85 doi: 10.1007/BF00484019
Isaacs WA.No abstract available
[Middle peptide sequence obtained by cleaving horse myoglobin with cyanogen bromide].
Bulletin de la Societe de chimie biologique    July 25, 1969   Volume 51, Issue 3 439-455 
Han K, Boulanger Y, Dautrevaux M, Biserte G.No abstract available
[Structure of peptides isolated from chymotrypsin hydrolysates of horse myoglobin].
Bulletin de la Societe de chimie biologique    January 30, 1969   Volume 50, Issue 10 1651-1669 
Boulanger Y, Dautrevaux M, Han K, Biserte G.No abstract available
Action of horse urinary kallikrein on synthetic derivatives of bradykinin.
Biochemical pharmacology    October 1, 1968   Volume 17, Issue 10 2232-2234 doi: 10.1016/0006-2952(68)90200-1
Babel I, Stella RC, Prado ES.Previous experiments indicated that horse urinary kallikrein (UK) hydrolyzes salminei- e and polyarginine, a but not polylysine. This paper reports the action of UK on bradykinyl-serine, methionyllysyl-bradykinin and lysyllysyl-bradykinin.
Comparative analysis of the IgG heavy chain carbohydrate peptide.
Journal of molecular biology    December 28, 1967   Volume 30, Issue 3 555-558 doi: 10.1016/0022-2836(67)90369-5
Howell JW, Hood L, Sanders BG.No abstract available