Arrangement of the disulphide bridges in human low-Mr kininogen

The arrangement of the disulphide bridges in human low-Mr kininogen has been elucidated. Low-Mr kininogen contains 18 half-cystine residues forming nine disulphide bridges. The first and the last half-cystine residues of the amino acid sequence form a disulphide loop which spans the heavy- and the light-chain portion of the kininogen molecule. The other 16 half-cystine residues are linked consecutively to form eight loops of 4-20 amino acids; these loops are lined up in the heavy-chain portion of the kininogen molecule. In this way, a particular pattern of disulphide loops is formed which seems to be of critical importance for the inhibitor function of human kininogen.

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Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

Zeitschrift für Naturforschung B ◽

10.1515/znb-1969-0716 ◽

1969 ◽

Vol 24 (7) ◽

pp. 877-885 ◽

Cited By ~ 16

Author(s):

H. G. Wittmann ◽

I. Hindennach ◽

B. Wittmann-Liebold

Keyword(s):

Experimental Data ◽

Amino Acids ◽

Amino Acid ◽

Coat Protein ◽

Amino Acid Sequence ◽

Spatial Structure ◽

Amino Acid Sequences ◽

The Other ◽

Tryptic Peptides ◽

Tmv Strains

Experimental data for determining a) the amino acid sequences of eight tryptic peptides containing 95 amino acids and b) the order of the tryptic peptides are given. Combining the data of this and of a previous paper the complete amino acid sequence of the coat protein of the TMV strain Holmes rib grass (HRG) is established (Fig. 5). It is compared with three other TMV strains the sequences of which have been determined before (Fig. 6).Differences and similarities between the sequences of the four TMV strains are discussed. HRG has a deletion of two amino acids and it is the most distantly related of the four TMV strains. When the sequence of HRG is compared to that of any of the other strains it turns out that in each case more than 50% of the 156 positions contain different amino acids (Fig. 7).The number of positions with the same amino acid in all strains and mutants so far studied is 30 per cent. These positions are not randomly distributed but clustered mainly in two regions. This finding probably reflects the restriction of amino acid exchanges by the spatial structure of the viral rod.

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Amino acid-sequence variability at the N-terminal extra piece of mouse immunoglobulin light-chain precursors of the same and different subgroups

Biochemical Journal ◽

10.1042/bj1570145 ◽

1976 ◽

Vol 157 (1) ◽

pp. 145-151 ◽

Cited By ~ 21

Author(s):

Y Burstein ◽

I Schechter

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Sequence ◽

Light Chain ◽

Variable Region ◽

Amino Acid Residues ◽

Free System ◽

Methionine Residue ◽

N Terminus ◽

Mouse Myeloma

The proteins programmed in the wheat-germ cell-free system by the mRNA coding for the MOPC-63 mouse myeloma L (light) chain were labelled with six radioactive amino acids: [35S]methionine, [4,5-3H]leucine, [3,4-3H]proline, [3-3H]serine, [4,5-3H]isoleucine or [2,3-3H]alanine. Amino acid-sequence analyses showed that over 90% of the total cell-free product was one homogeneous protein, which corresponds to the MOPC-63 L-chain precursor. In this precursor an extra piece, 20 amino acid residues in length, precedes the N-terminus of the mature L chain. The extra piece contains one methionine residue at the N-terminus, six leucine residues, which are clustered in two triplets at positions 6, 7, 8 and 11, 12, 13, one proline residue at position 16, and one serine residue at position 18. The closely gathered leucine residues, as well as their abundance (30%), suggest that the extra-piece moiety is hydrophobic. In the precursors, the extra piece is coupled to the variable region of the L chain. Partial sequences of precursors of L chains of the same and different subgroups that were labelled with the above six radioactive amino acids indicate that the extra piece is part of the variable region. Thus the precursors of MOPC-63 and MOPC-321 L chains, which are of the same subgroup, have extra pieces of identical size (20 residues), and so far their partial sequences are also identical (see above). On the other hand, in the precursor of MOPC-41 L chain, which is of a different subgroup, the extra piece is 22 residues in length. Further, the sequence of the MOPC-41 extra piece differs in at least ten positions from sequences of the extra pieces of the precursors of MOPC-63 and MOPC-321 L chains.

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Amino Acid Sequence of Trocarin, a Prothrombin Activator FromTropidechis carinatus Venom: Its Structural Similarity to Coagulation Factor Xa

Blood ◽

10.1182/blood.v94.2.621.414k25_621_631 ◽

1999 ◽

Vol 94 (2) ◽

pp. 621-631 ◽

Cited By ~ 1

Author(s):

Jeremiah S. Joseph ◽

Maxey C.M. Chung ◽

Kandiah Jeyaseelan ◽

R. Manjunatha Kini

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Blood Coagulation ◽

Snake Venom ◽

Heavy Chain ◽

Light Chain ◽

Critical Role ◽

Factor Xa ◽

Coagulation Factor ◽

Group Ii

Among snake venom procoagulant proteins, group II prothrombin activators are functionally similar to blood coagulation factor Xa. We have purified and partially characterized the enzymatic properties of trocarin, the group II prothrombin activator from the venom of the Australian elapid, Tropidechis carinatus (rough-scaled snake). Prothrombin activation by trocarin is enhanced by Ca2+, phospholipids, and factor Va, similar to that by factor Xa. However, its amidolytic activity on peptide substrate S-2222 is significantly lower. We have determined the complete amino acid sequence of trocarin. It is a 46,515-Dalton glycoprotein highly homologous to factor Xa and shares the same domain architecture. The light chain possesses an N-terminal Gla domain containing 11 γ-carboxyglutamic acid residues, followed by two epidermal growth factor (EGF)-like domains; the heavy chain is a serine proteinase. Both chains are likely glycosylated: the light chain at Ser 52 and the heavy chain at Asn 45. Unlike other types of venom procoagulants, trocarin is the first true structural homologue of a coagulation factor. It clots snake plasma and thus may be similar, if not identical, to snake blood coagulation factor Xa. Unlike blood factor Xa, it is expressed in high quantities and in a nonhepatic tissue, making snake venom the richest source of factor Xa-like proteins. It induces cyanosis and death in mice at 1 mg/kg body weight. Thus, trocarin acts as a toxin in venom and a similar, if not identical, protein plays a critical role in hemostasis.

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Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones

Biochemical Journal ◽

10.1042/bj2420849 ◽

1987 ◽

Vol 242 (3) ◽

pp. 849-856 ◽

Cited By ~ 81

Author(s):

C F Catterall ◽

A Lyons ◽

R B Sim ◽

A J Day ◽

T J R Harris

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Heavy Chain ◽

Light Chain ◽

Cdna Clones ◽

Serine Proteinases ◽

Human Complement ◽

Factor I ◽

Protein Factor ◽

Control Protein

A cDNA clone of the mRNA coding for the human complement system control protein Factor I has been isolated. The predicted amino acid sequence obtained from the DNA sequence demonstrates a protein consisting of a heavy chain (Mr 35,400) linked to a light chain (Mr 27,600), both of which contain three sites for N-linked glycosylation. The light chain has clear homology with other serine proteinases, most notably in the region of the catalytically active and structurally important amino acids and shares some of the features characteristic of the plasminogen activators. The heavy chain has a clear ‘mosaic’ nature typical of the plasma serine proteinases; in particular it contains class A and class B LDL (low-density lipoprotein) receptor repeats with conserved cysteine residues similar to those found in other complement proteins.

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Fine specificity of idiotope suppression in the A/J anti-azophenylarsonate response.

Journal of Experimental Medicine ◽

10.1084/jem.157.2.795 ◽

1983 ◽

Vol 157 (2) ◽

pp. 795-800 ◽

Cited By ~ 14

Author(s):

T L Rothstein ◽

M N Margolies ◽

M L Gefter ◽

A Marshak-Rothstein

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Heavy Chain ◽

Germ Line ◽

The Other ◽

Fine Specificity

Two hapten-inhibitable murine monoclonal antiidiotopic antibodies identified two idiotopes expressed by the heavy chain of hybridoma protein 36-65, whose amino acid sequence is encoded in the germ line of A/J mice. Among cross-reactive idiotype-positive hybridoma proteins and p-azophenylarsonate-immune antibodies, the two idiotopes were not always expressed together; some diversified antibodies expressed one idiotope without the other. Suppression that was induced by the two antiidiotopes was idiotope specific and corresponded to the fine specificities of these two reagents.

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Cryo-EM structure of the human heteromeric amino acid transporter b0,+AT-rBAT

Science Advances ◽

10.1126/sciadv.aay6379 ◽

2020 ◽

Vol 6 (16) ◽

pp. eaay6379 ◽

Cited By ~ 2

Author(s):

Renhong Yan ◽

Yaning Li ◽

Yi Shi ◽

Jiayao Zhou ◽

Jianlin Lei ◽

...

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Heavy Chain ◽

Light Chain ◽

Membrane Trafficking ◽

Binding Pocket ◽

Disulfide Bridge ◽

Ligand Molecule ◽

Amino Acid Transporters ◽

Cationic Amino Acids

Heteromeric amino acid transporters (HATs) catalyze the transmembrane movement of amino acids, comprising two subunits, a heavy chain and a light chain, linked by a disulfide bridge. The b0,+AT (SLC7A9) is a representative light chain of HATs, forming heterodimer with rBAT, a heavy chain which mediates the membrane trafficking of b0,+AT. The b0,+AT-rBAT complex is an obligatory exchanger, which mediates the influx of cystine and cationic amino acids and the efflux of neutral amino acids in kidney and small intestine. Here, we report the cryo-EM structure of the human b0,+AT-rBAT complex alone and in complex with arginine substrate at resolution of 2.7 and 2.3 Å, respectively. The overall structure of b0,+AT-rBAT exists as a dimer of heterodimer consistent with the previous study. A ligand molecule is bound to the substrate binding pocket, near which an occluded pocket is identified, to which we found that it is important for substrate transport.

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STRUCTURE OF HUMAN α2-PLASMIN INHIBITOR DEDUCED FROM THAT OF cDNA

10.1055/s-0038-1644371 ◽

1987 ◽

Author(s):

Y Sumi ◽

Y Nakamura ◽

M Sakai ◽

M Muramatsu ◽

N Aoki

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Sequence ◽

Stop Codon ◽

Amino Acid Sequences ◽

The Other ◽

Terminal Sequence ◽

Amino Terminal ◽

Carboxyl Terminal ◽

Plasmin Inhibitor

The complete amino acid sequence of α2-plasmin inhibitor (α2PI) was determined by cDNA cloning. A Agt 10 cDNA library was prepared from poly(A)+mRNA isolated from cultured human liver cells. The labeled oligonucleotides, corresponding to the reported partial amino acid sequences of α2PI, were used as probes to screen the library. One of the positive clones was subcloned into plasmid pUC8. A 2.2 kilobase cDNA clone thus isolated contains a region coding for a portion of a leader sequence, the mature protein, a stop codon (TGA), a 3' noncoding region (733 nucleotides), and a poly(A)tail (37 nucleotides). The amino acid sequence deduced from the cDNA is composed of 452 amino acids starting with an amino-terminal sequence of Asn-Gln-Glu-Gln and ending with a carboxyl-terminal sequence of Gly-Ser-Pro-Lys. The sequence shows approximately 30% homology with those of other plasma serine protease inhibitors. However, α2PI extends 50-52 amino acids beyond the carboxyl-terminal ends of the other inhibitors. This 50-52 carboxyl-terminal amino acid sequence is therefore specific to α2PI, and contains the sequence that is exactly the same as that of the peptide containing the plasminogen binding site. There are three lysine residues possibly involved in the binding to plasminogen in this region. From the homology with the other inhibitors, the inhibitor's reactive-site peptide bond was suggested to be Met-Ser and the same as that of ai-antitrypsin. The Met residue is located at the 362 position from the amino-terminal end.

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Amino Acid Sequence of Trocarin, a Prothrombin Activator FromTropidechis carinatus Venom: Its Structural Similarity to Coagulation Factor Xa

Blood ◽

10.1182/blood.v94.2.621 ◽

1999 ◽

Vol 94 (2) ◽

pp. 621-631 ◽

Cited By ~ 59

Author(s):

Jeremiah S. Joseph ◽

Maxey C.M. Chung ◽

Kandiah Jeyaseelan ◽

R. Manjunatha Kini

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Blood Coagulation ◽

Snake Venom ◽

Heavy Chain ◽

Light Chain ◽

Critical Role ◽

Factor Xa ◽

Coagulation Factor ◽

Group Ii

Abstract Among snake venom procoagulant proteins, group II prothrombin activators are functionally similar to blood coagulation factor Xa. We have purified and partially characterized the enzymatic properties of trocarin, the group II prothrombin activator from the venom of the Australian elapid, Tropidechis carinatus (rough-scaled snake). Prothrombin activation by trocarin is enhanced by Ca2+, phospholipids, and factor Va, similar to that by factor Xa. However, its amidolytic activity on peptide substrate S-2222 is significantly lower. We have determined the complete amino acid sequence of trocarin. It is a 46,515-Dalton glycoprotein highly homologous to factor Xa and shares the same domain architecture. The light chain possesses an N-terminal Gla domain containing 11 γ-carboxyglutamic acid residues, followed by two epidermal growth factor (EGF)-like domains; the heavy chain is a serine proteinase. Both chains are likely glycosylated: the light chain at Ser 52 and the heavy chain at Asn 45. Unlike other types of venom procoagulants, trocarin is the first true structural homologue of a coagulation factor. It clots snake plasma and thus may be similar, if not identical, to snake blood coagulation factor Xa. Unlike blood factor Xa, it is expressed in high quantities and in a nonhepatic tissue, making snake venom the richest source of factor Xa-like proteins. It induces cyanosis and death in mice at 1 mg/kg body weight. Thus, trocarin acts as a toxin in venom and a similar, if not identical, protein plays a critical role in hemostasis.

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Complete Covalent Structure of Human Platelet Factor 4

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657071 ◽

1979 ◽

Vol 42 (05) ◽

pp. 1652-1660 ◽

Cited By ~ 4

Author(s):

Francis J Morgan ◽

Geoffrey S Begg ◽

Colin N Chesterman

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Amino Acid ◽

Amino Acid Sequence ◽

Human Platelet ◽

Platelet Factor 4 ◽

Platelet Factor ◽

Disulphide Bonds ◽

Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

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C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19801144 ◽

1980 ◽

Vol 45 (4) ◽

pp. 1144-1154 ◽

Cited By ~ 3

Author(s):

Miroslav Baudyš ◽

Helena Keilová ◽

Vladimír Kostka

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

The Other ◽

Terminal Sequence ◽

Terminal Part ◽

Terminal Amino Acid ◽

Tryptic Peptides ◽

Terminal Amino ◽

High Degree ◽

Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

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