Analisis Perilaku Pelanggan terhadap Tawaran Produk Perhiasan Emas pada PT. Pegadaian (Persero) Cabang Manado Utara

Perusahaan perlu mengetahui perilaku konsumen dalam menjalankan suatu usaha, untuk membantu mengembangkan usahanya sehingga dapat menentukan harga, promosi dan mendistribusikan barang secara baik. Tujuan penelitian untuk mengetahui pengaruh perilaku konsumen pada tawaran produk perhiasan emas dari PT. Pegadaian (Persero) Cabang Manado Utara. Penelitian ini menggunakan metode kualitatif yang berfokus pada perilaku konsumen. Hasil penelitian, sebagian besar konsumen yang membeli produk perhiasan emas pada PT. Pegadaian (Persero) berusia 39 sampai 57 tahun. Banyaknya pelanggan yang melakukan pembelian emas di umur 39 tahun keatas menunjukkan bahwa semakin bertambahnya umur semakin besar minat pelanggan dalam melakukan pembelian emas. Sebagian pelanggan PT. Pegadaian (Persero) melakukan pembelian emas karena keinginan dari diri sendiri tanpa adanya dorongan atau paksaan dari orang lain. Dalam melakukan tawaran produk perhiasan emas sebaiknya PT. Pegadaian (Persero) lebih menekankan pada perilaku pelanggan yaitu melihat apa yang menjadi motivasi, persepsi pelanggan mengenai emas, dan pengetahuan dengan memberikan penjelasan mengenai emas itu sendiri sehingga pelanggan tidak merasa dirugikan dan memiliki keyakinan sehingga dapat mengambil sikap untuk melakukan pembelian emas. Kata kunci: perilaku konsumen, perhiasan ema

MOLOKLUSI PADA GIGI CAMPURAN DAN PERAWATANNYA

XVII,52hlm

Entropically driven MHC class I recognition by human inhibitory receptor leukocyte Ig-like receptor B1 (LILRB1/ILT2/CD85j).

The human inhibitory receptor, leukocyte immunoglobulin (Ig)-like receptor B1 (also called Ig-like transcript (ILT) 2, CD85j), is broadly expressed on leukocytes. LILRB1 binds to a wide range of major histocompatibility complex class I molecules (MHCIs) and transduces negative signals that can, for example, prevent killing of MHCI-expressing cells. Here we report the kinetic, thermodynamic, NMR and crystallographic analyses of MHCI recognition by LILRB1. Kinetic studies demonstrated that LILRB1 binds to MHCIs with fast association and dissociation rates, typical of cell-cell recognition receptors. Thermodynamic analyses showed that LILRB1-MHCI interactions are entropically driven (-TdeltaS = -9.4 approximately -6.6 kcal mol(-1)) with low heat capacity changes (deltaC(p) = -0.22 approximately -0.10 kcal mol(-1) K(-1)). The crystal structures of LILRB1 in the different crystal forms exhibited variation in the elbow angle between the two N-terminal Ig-like domains, indicating interdomain flexibility. Consistently, NMR analysis provided the direct evidence of the conformational changes of LILRB1 upon the MHCI binding. These findings suggest that LILRB1-MHCI interactions, while involving some conformational adjustment, are not accompanied by a very large reduction in conformational flexibility at the binding interface. This mode of binding is distinct from "induced-fit" binding, which is associated with large reductions in conformational flexibility, and would be suitable for rapid engagement of MHCIs to enable fast monitoring of the expression level of MHCIs on target cells

Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d)

HLA-G is a nonclassical MHC class I (MHCI) molecule that can suppress a wide range of immune responses in the maternal–fetal interface. The human inhibitory immune receptors leukocyte Ig-like receptor (LILR) B1 [also called LIR1, Ig-like transcript 2 (ILT2), or CD85j] and LILRB2 (LIR2/ILT4/CD85d) preferentially recognize HLA-G. HLA-G inherently exhibits various forms, including β(2)-microglobulin (β(2)m)-free and disulfide-linked dimer forms. Notably, LILRB1 cannot recognize the β(2)m-free form of HLA-G or HLA-B27, but LILRB2 can recognize the β(2)m-free form of HLA-B27. To date, the structural basis for HLA-G/LILR recognition remains to be examined. Here, we report the 2.5-Å resolution crystal structure of the LILRB2/HLA-G complex. LILRB2 exhibits an overlapping but distinct MHCI recognition mode compared with LILRB1 and dominantly recognizes the hydrophobic site of the HLA-G α3 domain. NMR binding studies also confirmed these LILR recognition differences on both conformed (heavy chain/peptide/β(2)m) and free forms of β(2)m. Binding studies using β(2)m-free MHCIs revealed differential β(2)m-dependent LILR-binding specificities. These results suggest that subtle structural differences between LILRB family members cause the distinct binding specificities to various forms of HLA-G and other MHCIs, which may in turn regulate immune suppression