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Biomedical subjects

M Bajaj

Publications and source records attributed to M Bajaj.

30 records · Page 2Linked to original sources
PubMed1993

Studies on the development of high-protein biscuits from composite flours.

Composite flours prepared from wheat, greengram, bengalgram and blackgram flours were studied for the preparation of biscuits. Protein content of biscuits increased as the level of the pulse flours increased. Wheat flour containing bengalgram and blackgram flours adversely affected the top grain, texture and colour of biscuits. Biscuits made with higher levels of bengalgram (more than 15%) were tough and difficult to break and required higher compression force. Addition of greengram flour did not significantly affect top grain, texture and colour of biscuits. The biscuits made from 15% greengram supplemented wheat flour scored the highest for flavour characteristics. Thickness, diameter and spread ratio of biscuits containing different levels of pulse flours were significantly different from control sample. Sensory evaluation scores showed that acceptable biscuits can be prepared from wheat flour supplemented with these pulse flours at a level of 15 percent.

Carbohydrates↗
PubMed1991

Studies on the development of nutritious cookies utilizing sunflower kernels and wheat germ.

Wheat germ and sunflower kernels were substituted at a level of 0, 5, 10, 15, 20, 25 and 30 percent of wheat flour for the preparation of cookies. The crude protein, ash and crude fiber contents increased with the addition of sunflower kernels. Similarly, with the addition of wheat germ, protein, ash and crude fibre contents increased significantly. The cookies containing 30% wheat germ and 20 percent sunflower kernels were found to be superior in overall acceptability.

Dietary Fiber↗
PubMed1987

On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors.

Alignment of the sequences, the identification of conserved residue patterns and secondary structure predictions indicate that the extra-cellular regions of the human and Drosophila epidermal growth factor (EGF), c-erb-B2 and human insulin receptors each contain two large, homologous domains (L) which are probably comprised of at least four short alpha-helices followed by turns of conserved length and beta-strands. In the human and Drosophila EGF and c-erb-B2 receptors these homologous domains are each followed by a series of smaller cystine-rich domains (S) to give a gene-duplicated structure of L1S11S12S13L2S21S22S23. In the human insulin receptor, the second series of cystine domains is replaced by a different sequence. These duplicated structures are probably organised as a pseudo-symmetrical dimer. There are two 'hyper-variable' regions, one at the end of the large domains and one in the cystine-rich sequences, which are candidates for hormone or growth-factor binding.

Amino Acid Sequence↗
PubMed1986

Coypu insulin. Primary structure, conformation and biological properties of a hystricomorph rodent insulin.

Insulin from a hystricomorph rodent, coypu (Myocaster coypus), was isolated and purified to near homogeneity. Like the other insulins that have been characterized in this Suborder of Rodentia, coypu insulin also exhibits a very low (3%) biological potency, relative to pig insulin, on lipogenesis in isolated rat fat-cells. The receptor-binding affinity is significantly higher (5-8%) in rat fat-cells, in rat liver plasma membranes and in pig liver cells, indicating that the efficacy of coypu insulin on receptors is about 2-fold lower than that of pig insulin. The primary structures of the oxidized A- and B-chains were determined, and our sequence analysis confirms a previous report [Smith (1972) Diabetes 21, Suppl. 2, 457-460] that the C-terminus of the A-chain is extended by a single residue (i.e. aspartate-A22), in contrast with most other insulin sequences, which terminate at residue A21. In spite of a large number of amino acid substitutions (relative to mammalian insulins), computer-graphics model-building studies suggest a similar spatial arrangement for coypu insulin to that for pig insulin. The substitution of the zinc-co-ordinating site (B10-His----Gln) along with various substitutions on the intermolecular surfaces involved in the formation of higher aggregates are consistent with the observation that this insulin is predominantly 'monomeric' in nature. The c.d. spectrum of coypu insulin is relatively similar to those of casiragua insulin and of bovine insulin at low concentration.

Amino Acid Sequence↗
PubMed1985

The conformation of insulin-like growth factors: relationships with insulins.

The insulin-like growth factors and hystricomorph insulins have been modelled by interactive computer graphics on the assumption that their sequence homology to insulin implies that they will have a similar tertiary structure. These studies suggest that, although the insulin-related molecules can adopt the insulin fold, they are unlikely to form hexamers and if they form dimers they will be of reduced stability. The non-suppressibility of insulin-like growth factors by anti-insulin antibodies is explained in terms of differences of surface residues in the region A8-A10 and B1-B5. Receptor affinity of insulins and insulin-like growth factors for insulin receptors is explicable in terms of a receptor-binding site in the vicinity of B25 Phe on the insulin surface. An equivalent region around B25 Tyr of insulin-like growth factors may be responsible for their binding to type 1 receptors, although binding type 2 receptors must involve a different surface region not shared by insulin.

Amino Acid Sequence↗
PubMed1984

Evolution in the insulin family: molecular clocks that tell the wrong time.

The sequences, three-dimensional structures and biological activities of insulins and the related insulin-like growth factors demonstrate many changes that have occurred in evolution. In the hystricomorph rodent insulins this has led to insulins which differ not only from those of other mammals but also amongst themselves. They show no single characteristic substitution but generally exhibit reduced anabolic activity, increased growth promoting effects and inability to form oligomers. Their divergence is discussed in terms of orthologous evolution implying very variable rates of accepted mutations, and paralogous evolution for which a minimal hypothesis must be several silently evolving genes.

Amino Acid Sequence↗
PubMed1983

Dogfish insulin. Primary structure, conformation and biological properties of an elasmobranchial insulin.

Insulin from an elasmobranch, the spiny dogfish (Squalus acanthias) has been purified to near homogeneity by means of acid-ethanol extraction and salt precipitation. The amino acid sequences of the performic-acid-oxidised A and B chains have been determined and exhibit some unusual features. The A chain contains a total of 22 amino acids; only the insulin from coypu (a member of the Rodentia suborder, Hystricomorpha), has previously been reported to contain an extension past the A21 asparagine. The B10 histidine, which is involved in the formation of the insulin hexamers in higher vertebrates through the co-ordination of zinc, is present in this elasmobranch insulin. Several substitutions relative to bovine insulin occur in the proposed receptor binding region (A5Gln leads to His, B21Glu leads to Pro, B22Arg leads to Lys, B25Phe leads to Tyr). In spite of these substitutions, the maximal response in the rat epididymal fat cell assay is the same for bovine and dogfish insulins; the concentration required to produce the half-maximal response is, however, approximately threefold greater for dogfish insulin than that of bovine insulin. The use of interactive computer graphics model-building predicts that the dogfish insulin can attain a three-dimensional structure very similar to that of bovine insulin; circular dichroic spectra are presented which support the model-building studies.

Adipose Tissue↗