Search PubMed⌕ Search

Biomedical subjects

Z H Zaidi

Publications and source records attributed to Z H Zaidi.

At least 37 records · Page 2Linked to original sources

Extensive multiplicity of the miscellaneous type of neurotoxins from the venom of the cobra Naja naja naja and structural characterization of major components.

A multiplicity of miscellaneous type neurotoxins were detected in the venom of the cobra Naja naja naja by use of reverse-phase HPLC and FPLC. The primary structures of major forms were determined, giving 4 novel structures. All four contain 62-65 residues, with 10 half-cystine residues and resemble the miscellaneous type of toxins from other Naja species. Differences within the species are extensive, exchanges occur at 27 positions, giving only 58% residue identity between all forms. However, the differences are largely limited to 3 regions corresponding to structurally important loops where two functional residues participating in receptor binding are exchanged. The four miscellaneous neurotoxins now characterized, together with the minor components of the miscellaneous type, the minimally four neurotoxins reported before, and other related toxins, indicate the existence of an extensive toxin gene multiplicity.

Amino Acid Sequence↗

Characterization of phospholipase A2 from the venom of Horned viper (Cerastes cerastes).

Phospholipase A2 has been purified from the venom of Horned viper (Cerastes cerastes) by gel permeation chromatography followed by reverse-phase HPLC. The primary structure was established by sequence analysis of the intact protein and its enzymic peptides. The structure has 120 residues, properties like other group IIB phospholipases, but only 45-55% identity with the enzyme from other viperid species, and large variations even within the species (26% residue differences at known positions in another form).

Amino Acid Sequence↗

Primary structure of hemoglobin alpha-chain from cuckoo (Eudynamys scolopaceae, cuculiformes).

The complete amino acid sequence of the alpha A-chain of major hemoglobin component from Cuckoo (Eudynamys scolopaceae) is presented. Separation of the polypeptide subunits was achieved by ion exchange chromatography in the presence of 8 M urea. The sequence was studied by automatic Edman degradation of the native chain and its tryptic fragments in a gas-phase sequencer. Comparison with other avian hemoglobins shows residues alpha 21, alpha 30, alpha 96, alpha 110, and alpha 114 as being specific to Cuckoo. The functional significance of these is discussed.

Amino Acid Sequence↗

Primary structure of hemoglobin beta-chain from Columba livia (gray wild pigeon).

Primary structure of beta-chain of pigeon is presented. It was determined by amino acid sequence analysis of intact beta-chain and its peptides obtained by the enzymatic and chemical cleavage. Comparison of amino acid sequence of the chain with other available data shows beta 14 Ile, beta 61 Lys, and beta 113 Ile as residues specific to pigeon. One important replacement at alpha 1 beta 1 contact is beta 55 Met----Ser.

Amino Acid Sequence↗

Biochemical building blocks of a lepidopteran insect, Schoenobius inotata.

Schoenobius inotata, a pheromone producing insect, commonly known as rice stem borer, was studied for its biochemical composition namely lipid, carbohydrate and amino acids. The studies involved the application of column, thin layer and gas liquid chromatography besides mass and proton magnetic resonance spectrometry. Amino acid analysis was performed on automatic amino acid analyser. No such report on this species has so far appeared.

Journal Article↗

Primary structure and functional properties of cobra (Naja naja naja) venom Kunitz-type trypsin inhibitor.

A trypsin inhibitor from the venom of the cobra Naja naja naja has been isolated by a single step of reverse-phase high-performance liquid chromatography. The protein strongly inhibits trypsin (Ki = 3.5 pM). The primary structure was determined by peptide analysis of the [14C]carboxymethylated inhibitor. The 57-residue polypeptide chain belongs to the family of Kunitz-type inhibitors, and exhibits 42% residue identity with bovine pancreatic trypsin inhibitor. The structure shows only 70% identity with the corresponding peptide from the Capa cobra (Naja nevia), establishing that the inhibitor molecule exhibits extensive variations. Functionally, a basic residue at position P3' correlates with strong inhibition.

Amino Acid Sequence↗

Purification and characterization of a chymotrypsin Kunitz inhibitor type of polypeptide from the venom of cobra (Naja naja naja).

A chymotrypsin Kunitz inhibitor type of polypeptide has been isolated from the venom of Naja naja naja by reverse phase HPLC and cation exchange FPLC. It is present in a considerably lower amount than that of the corresponding trypsin inhibitor. The primary structure, determined by sequence analysis of the whole molecule and its tryptic peptides, has 57 residues with an apparent molecular mass of 6.2 kDa. The main contact site with the protease (P1) has a Phe, showing the specificity of the inhibitor. Of residues considered functionally important in Kunitz-type inhibitors, Gly-36 is replaced by Ser in a segment of weak contacts with the protease.

Amino Acid Sequence↗

Characterization of a cytotoxin-like basic protein from the cobra (Naja naja naja) venom.

A cytotoxin-like basic protein has been isolated from the venom of the nominate race of cobra (Naja naja naja from Pakistan) by a single step of high-performance liquid chromatography. The primary structure was determined and consists of 62 amino acid residues in a single polypeptide chain. It is highly similar to that of the cytotoxin-like basic proteins isolated from other Naja species, but differs in two of the SS-loop structures from that of cytotoxins.

Amino Acid Sequence↗

Sea snake (Microcephalophis gracilis) hemoglobin: primary structure and relationships to other forms.

The hemoglobin of the sea snake Microcephalophis gracilis was purified and the primary structure of the alpha and beta chains determined. This is the first sea snake hemoglobin structure characterized, and apparently also the first complete structure of any snake hemoglobin (an alpha chain of a viper was known), allowing judgments of reptilian variants. Variations between the sea snake form and other reptilian forms are large (52-65 differences for the alpha chains), of similar order as those between the sea snake and avian (56-65 differences) or human (58 differences) forms. Functionally, 19 residues at alpha/beta contact areas and 7 at heme contacts are exchanged in relation to the human alpha and beta chains. Four positions of the sea snake hemoglobin contain residues thus far unique to this form. However, all replacements appear compatible with conserved overall functional properties.

Amino Acid Sequence↗

Characterization of two different peptides from the venom of the scorpion Buthus sindicus.

Two disulfide-rich, low-molecular mass peptides (approximately 3 kDa and approximately 4 kDa) have been isolated from Buthus sindicus venom using ion-exchange and reverse-phase HPLC. Peptide I has 35 residues with 8 half-cystine residues and is clearly related to four-disulfide core proteins of the neurophysin type and to toxins of other scorpion species (55-63% residue identity). Peptide II, present in low yield, has 28 residues with 6 half-cystine residues and a structure largely dissimilar from that of peptide I and other characterized toxins, although probably still a member of the disulfide core peptide type. Consequently, scorpion venom contains, in addition to toxins characterized before, toxin-like compounds with distant relationships.

Amino Acid Sequence↗

Primary structure of hemoglobin alpha-chain of Columba livia (gray wild pigeon).

Primary structure of hemoglobin of alpha-chain of Columba livia is presented. The separation of alpha-chain was obtained from globin by ion-exchange chromatography (CMC-52) and reversed-phase HPLC (RP-2 column). Amino acid sequence of intact as well as tryptic digested chain was determined on gas-phase sequencer. Structure is aligned homologously with 21 other species. Among different exchanges, positions alpha 24 (Tyr----Leu), alpha 26 (Ala----Gly), alpha 32 (Met----Leu), alpha 64 (Asp----Glu), alpha 113 (Leu----Phe), and alpha 129 (Leu----Val) are unique to pigeon hemoglobin. The various exchanges in alpha-chain are discussed with reference to evolution and phylogeny. The results show that the order Columbiformes is evolutionarily closer to the order Anseriformes. Since the pigeon is homogeneous, having HbA (alpha A-chain) and lacks alpha D-chain, its phylogenetic placement could be established among birds having single hemoglobin components.

Amino Acid Sequence↗

Primary structure of hemoglobin from gray partridge (Francolinus pondacerianus, Galliformes).

The complete amino acid sequence of the alpha A-chain of major hemoglobin component from gray partridge Francolinus pondacerianus is presented. The major component HbA accounts for 75% of the total hemolysate. Separation of the globin subunits was achieved by ion-exchange chromatography on CM-Cellulose in 8 M urea. The sequence was studied by automatic Edman degradation of the native chain and its tryptic peptides in a gas-phase sequencer. The phylogenetic relationship of Galliformes with other avian orders is discussed.

Amino Acid Sequence↗

Primary structure of the hemoglobin beta-chain of rose-ringed parakeet (Psittacula krameri).

The primary structure of Rose-ringed Parakeet hemoglobin beta-chain was established, completing the analysis of this hemoglobin. Comparison with other avian beta-chains show variations smaller than those for the corresponding alpha-chains. There are 11 amino acid exchanges in relationship to the only other characterized psittaciform beta-chain, and a total of 35 positions are affected by differences among all avian beta-chains analyzed (versus 61 for the alpha-chains). At three positions, the Psittacula beta-chain has residues unique to this species. Three alpha 1 beta 1 contacts are modified, by substitutions at positions beta 51, beta 116, and beta 125.

Amino Acid Sequence↗

Phospholipase A2 from cobra (Naja naja naja) venom. Primary structure and subspecies variation.

The primary structure of phospholipase A2 of the major race of Indian cobra has been determined. Together with previous data on other subforms, it establishes subspecies variations at no less than 20 of the 119 positions in the protein. These variations are large, not only in number but in several cases also regarding properties of the residues involved. Nevertheless, all structures are compatible with largely unaltered enzyme properties.

Amino Acid Sequence↗

Primary structure of the hemoglobin alpha-chain of rose-ringed parakeet (Psittacula krameri).

The structure of the hemoglobin alpha-chain of Rose-ringed Parakeet was determined by sequence degradations of the intact subunit, the CNBr fragments, and peptides obtained by digestion with staphylococcal Glu-specific protease and trypsin. Using this analysis, the complete alpha-chain structure of 21 avian species is known, permitting comparisons of the protein structure and of avian relationships. The structure exhibits differences from previously established avian alpha-chains at a total of 61 positions, five of which have residues unique to those of the parakeet (Ser-12, Gly-65, Ser-67, Ala-121, and Leu-134). The analysis defines hemoglobin variation within an additional avian order (Psittaciformes), demonstrates distant patterns for evaluation of relationships within other avian orders, and lends support to taxonomic conclusions from molecular data.

Amino Acid Sequence↗

Characterization of a heterogeneous camel milk whey non-casein protein.

A milk protein, occurring in the whey fraction, has been characterized from camel milk. Determination of the primary structure reveals the existence of two related types of chain with residue differences in at least the N-terminal region. A fragment representing an N-terminal part of the protein was also recovered (heterogeneous at the same positions). The absence of cysteine residues in the protein shows that no disulphide bridges are present. The pattern of fragments and a parent protein resembles that for casein and its fragments, showing that fragments and a multiplicity of forms may be typical for different milk proteins.

Amino Acid Sequence↗

Partial sequence of hemoglobin from cobra (Naja naja naja).

Hemoglobin from the cobra snake, Naja naja naja, was isolated and its chains separated on a CM-cellulose column. The separation profile revealed an alpha and two beta chains having the molar proportions of [alpha]2[beta 1]1[beta 2]1. The N-terminal amino acid sequence of the intact chains and of the CNBr peptides were carried out. The beta 2 chain was found to be heterogeneous comprising a minor component amounting to 11%. This later showed changes at two positions 9 and 14 in the first 30 residues sequenced.

Amino Acid Sequence↗